Citations 17
Rab32 regulates Golgi structure and cell migration through Protein Kinase A–mediated phosphorylation of Optineurin
Johnson, Katherine M. , Marley, Maxwell G., Cao, Hong , Mostafa, Nourhan, McNiven, Mark A. , Drizyte-Miller, Kristina , Razidlo, Gina L , Johnson, Katherine M., Drizyte‐Miller, Kristina , Chen, Jing , Schott, Micah B. , Razidlo, Gina L.
Proceedings of the National Academy of Sciences | April 21, 2025 | Volume: 122 | Issue: 17 | Pages: No page available
Rab32 is a small GTPase and molecular switch implicated in vesicular trafficking. Rab32 is also an A-Kinase Anchoring Protein (AKAP), which anchors cAMP-dependent Protein Kinase (PKA) to specific subcellular locations and specifies PKA phosphorylation of nearby substrates. Surprisingly, we found that a form of Rab32 deficient in PKA binding (Rab32 L188P) relocalized away from the Golgi apparatus and induced a marked disruption in Golgi organization, assembly, and dynamics. Although Rab32 L188P did not cause a global defect in PKA activity, our data indicate that Rab32 facilitates the phosphorylation of a specific PKA substrate. We uncovered a direct interaction between Rab32 and the adaptor protein optineurin (OPTN), which regulates Golgi dynamics. Further, our data indicate that optineurin is phosphorylated by PKA at Ser342 in a Rab32-dependent manner. Critically, blocking phosphorylation at OPTN Ser342 leads to Golgi fragmentation, and a phospho-mimetic version of OPTN rescues Golgi defects induced by Rab32 L188P. Finally, Rab32 AKAP function and OPTN phosphorylation are required for Golgi repositioning during cell migration, contributing to tumor cell invasion. Together, these data reveal a role for Rab32 in regulating Golgi dynamics through PKA-mediated phosphorylation of OPTN.
AKAP12 variant 1 knockout enhances vascular endothelial cell motility
Ali, Ashrifa, Grove, Bryon D. , Roy, Bhaskar, Schott, Micah B.
No container title available | February 3, 2025 | Volume: No volume available | Issue: No issue available | Pages: No page available
Abstract In this study, we examined the role of AKAP12, in endothelial cell motility, with a specific focus on AKAP12 variants AKAP12v1 and AKAP12v2. Previous work has shown that AKAP12, a multivalent A-kinase anchoring protein that binds to PKA and several other proteins regulating protein phosphorylation, is expressed at low levels in most endothelia in vivo but at higher levels in cells in vitro . Here, we found that AKAP12 expression in endothelial cell (HUVEC) cultures was cell density-dependent, with the expression being highest in subconfluent cultures and lowest in confluent cultures. AKAP12 expression was also elevated in cells at the wound edge of wounded endothelial cell monolayers. Knockdown of variants 1 and 2 inhibited cell migration, whereas CRISPR/Cas9 knockout of AKAP12v1 enhanced migration, indicating that the absence of this variant and the presence of AKAP12v2 may shift the signaling pathways. Further analysis using bulk RNA sequencing revealed that the loss of AKAP12v1 affects genes associated with cell migration and intercellular junctions. We propose that AKAP12v1 and AKAP12v2 work together to modulate endothelial cell migration, providing insights into their distinct yet complementary roles in endothelial function and potential implications for cardiovascular health.
Ethanol disrupts hepatocellular lipophagy by altering Rab5-centric LD-lysosome trafficking
Schott, Micah B. , Rozeveld, Cody N., Bhatt, Saumya , Crossman, Bridget, Krueger, Eugene W. , Weller, Shaun G. , Rasineni, Karuna , McNiven, Mark A. , Schott, Micah B , Crossman, Bridget E. , Casey, Carol A.
Hepatology Communications | May 23, 2024 | Volume: 8 | Issue: 6 | Pages: No page available
Background:Previous reports suggest that lipid droplets (LDs) in the hepatocyte can be catabolized by a direct engulfment from nearby endolysosomes (microlipophagy). Further, it is likely that this process is compromised by chronic ethanol (EtOH) exposure leading to hepatic steatosis. This study investigates the hepatocellular machinery supporting microlipophagy and EtOH-induced alterations in this process with a focus on the small, endosome-associated, GTPase Rab5.Methods and Results:Here we report that this small Ras-related GTPase is a resident component of LDs, and its activity is important for hepatocellular LD-lysosome proximity and physical interactions. We find that Rab5 siRNA knockdown causes an accumulation of LDs in hepatocytes by inhibiting lysosome dependent LD catabolism. Importantly, Rab5 appears to support this process by mediating the recruitment of early endosomal and or multivesicular body compartments to the LD surface before lysosome fusion. Interestingly, while wild-type or a constituently active GTPase form (Q79L) of Rab5 supports LD-lysosome transport, this process is markedly reduced in cells expressing a GTPase dead (S34N) Rab5 protein or in hepatocytes exposed to chronic EtOH.Conclusions:These findings support the novel premise of an early endosomal/multivesicular body intermediate compartment on the LD surface that provides a “docking” site for lysosomal trafficking, not unlike the process that occurs during the hepatocellular degradation of endocytosed ligands that is also known to be compromised by EtOH exposure.
Hepatic lipolysis by β‐adrenergic stimulation is inhibited by ethanol exposure
Weller, Shaun G. , McNiven, Mark A. , Schott, Micah B. , Rasineni, Karuna , Schulze, Ryan J. , Casey, Carol A.
The FASEB Journal | November 26, 2023 | Volume: 31 | Issue: S1 | Pages: No page available
10.1096/fasebj.31.1_supplement.390.2
Steatotic hepatocytes accumulate profound numbers of large neutral lipid‐storage organelles called lipid droplets (LDs). The process by which the formation or utilization of these organelles are perturbed during NAFLD and NASH is poorly defined. EtOH consumption can also exacerbate these conditions markedly by yet unknown mechanisms. Thus, there is a critical need to understand lipolytic mechanisms for LD catabolism in hepatocytes. In adipocytes, catecholamines induce lipolysis through a β‐adrenergic/cAMP pathway that activates cytosolic lipases ATGL and HSL to catabolize LD triglycerides. Importantly, β‐adrenergic induction of LD catabolism has not been demonstrated in hepatocytes. Thus, the GOAL of this study was to determine whether hepatocytes, like adipocytes, also undergo cAMP‐mediated lipolysis in response to β‐adrenergic (β‐AR) stimulation. First, treatment of primary rat hepatocytes or Hep3B human hepatoma cells with the β‐AR agonist isoproterenol caused a 20–40% reduction in total cellular LD content within 24 hours. β‐AR induced LD loss was mimicked by the cAMP agonist forskolin/IBMX and was abrogated by the cAMP‐dependent protein kinase (PKA) inhibitor H89. In correlation, PKA activation following β‐AR stimulation was confirmed by FRET biosensors and biochemical analysis. β‐AR stimulation directly activated the lipolytic pathway, as evidenced by cAMP/PKA‐mediated phosphorylation of hormone sensitive lipase (HSL) and adipose triglyceide lipase (ATGL). In addition, pharmacological inhibitors against ATGL or HSL each blocked β‐AR induced LD loss, suggesting that lipase activation is critical for this process in stimulated cells. To examine whether β‐AR/cAMP stimulation triggered lipase recruitment directly to the LD, live‐cell imaging of Hep3B cells expressing either ATGL‐EGFP or HSL‐sfGFP showed that within 60 min of stimulation, each lipase was significantly displaced from the cytosol and recruited to the LD surface. This recruitment was blocked by the PKA inhibitor H89. Finally, to test if EtOH exposure attenuates the activation of lipolysis in hepatocytes, we isolated primary hepatocytes from rats fed a 6‐week ethanol‐containing Lieber‐DeCarli diet. Compared with controls, ethanol‐exposed hepatocytes showed a drastic inhibition in lipase activation and LD breakdown following β‐AR/cAMP stimulation. Remarkably, in ethanol‐metabolizing VA13 hepatocytes, ethanol insult completely prevented isoproterenol‐induced translocation of ATGL‐EGFP to the LD. In summary , these results show that β‐adrenergic stimulation mobilizes cytosolic lipases for LD breakdown in hepatocytes, and perturbation of this pathway could be a major consequence of chronic ethanol insult leading to fatty liver. Manipulation of this regulatory cascade could be useful in developing new therapies to attenuate fatty liver disease. Support or Funding Information This study was generously supported by funding from NIAAA 5R01AA020735 (MAM and CAC) and NIDDK 5R37DK044650 (MAM), T32DK007352‐36 (MBS), and P30DK084567 (Mayo Clinic Center for Cell Signaling in Gastroenterology).
Microautophagy catabolizes lipid droplets in liver hepatocytes via the small GTPase Rab5 and is connected to alcoholic fatty liver
Rozeveld, Cody N., Mehall, Bridget, McNiven, Mark A., Casey, Carol A. , Schott, Micah B.
The FASEB Journal | May 3, 2022 | Volume: 36 | Issue: S1 | Pages: No page available
10.1096/fasebj.2022.36.s1.r3458
Introduction and Objective Alcohol consumption has increased dramatically in recent years, representing a significant challenge to human health in metabolic disease. The leading cause of alcohol‐related death is alcohol‐associated liver disease (AALD), which is present at early stages (i.e. steatosis) in 90% of heavy drinkers. During early AALD, liver hepatocytes accumulate large stores of triglycerides in the form of lipid droplets (LDs). Under normal conditions, degradative lysosomes form direct contacts with LDs and catabolize lipid via microlipophagy, a specialized autophagic pathway utilizing the lipid‐degrading enzyme lysosomal acid lipase (LAL). However, the trafficking mechanisms that govern LD‐lysosome contacts during microlipophagy are poorly understood. Several promising candidates exist within the Rab family of small GTPases, which are well‐known to direct the trafficking of intracellular vesicles and LDs. Moreover, previous studies suggest that Rab proteins play central roles in LD catabolism. Thus, the OBJECTIVE of this study was to investigate novel Rab proteins that might be impaired by EtOH leading to altered LD dynamics and microautophagy. Materials and Methods To this end, we utilized RNAi gene silencing, subcellular fractionation, Western blot analysis, and high‐resolution microscopy to define Rabs that might target LDs to lysosomes during microlipophagy. To mimic alcoholic fatty liver, cellular and animal models of alcohol consumption were also used. Changes in LD‐lysosome interaction were measured by quantitative confocal microscopy following pharmacological inhibition of LAL by LAListat. Results First, confocal microscopy revealed that GFP‐Rab5, an early endosomal Rab GTPase, localizes to hepatocellular LDs consistent with proteomic and Western blot analyses showing abundant levels of Rab5 in biochemically isolated LDs. Importantly, siRNA knockdown of Rab5 in cultured hepatocytes showed substantial increases in total LD area (2‐fold) and LD number (1.6‐fold), and also blocked the catabolism of LDs in lipid‐loaded cells. Finally, Rab5 knockdown nearly completely abolished microlipophagy as measured by fluorescent LD accumulation in lysosomes following LAListat treatment. The dissociation of LDs from lysosomes in Rab5 knockdown cells was strikingly similar to the defect observed in EtOH‐fed hepatocytes. Together, these findings suggest that Rab5 is a key mediator of targeting LDs to the lysosome compartment for catabolism and may be a target of EtOH insult. Significance/Implication This study sheds light on new molecular mechanisms of microlipophagy that are affected by chronic alcohol consumption. These mechanisms may represent promising avenues for future therapeutic development toward mitigating hepatic steatosis and slowing the progression of AALD.
Lipophagy at a glance
Schott, Micah B. , Rozeveld, Cody N., Weller, Shaun G. , McNiven, Mark A. , Schott, Micah B
Journal of Cell Science | March 9, 2022 | Volume: 135 | Issue: 5 | Pages: No page available
ABSTRACT Lipophagy is a central cellular process for providing the cell with a readily utilized, high energy source of neutral lipids. Since its discovery over a decade ago, we are just starting to understand the molecular components that drive lipophagy, how it is activated in response to nutrient availability, and its potential as a therapeutic target in disease. In this Cell Science at a Glance article and the accompanying poster, we first provide a brief overview of the different structural and enzymatic proteins that comprise the lipid droplet (LD) proteome and reside within the limiting phospholipid monolayer of this complex organelle. We then highlight key players in the catabolic breakdown of LDs during the functionally linked lipolysis and lipophagy processes. Finally, we discuss what is currently known about macro- and micro-lipophagy based on findings in yeast, mammalian and other model systems, and how impairment of these important functions can lead to disease states.
Sequential lipolysis and lipophagy pathways orchestrate lipid droplet breakdown in hepatocytes
Weller, Shaun G. , McNiven, Mark A. , Schott, Micah B. , Schulze, Ryan J.
The FASEB Journal | June 21, 2021 | Volume: 33 | Issue: S1 | Pages: No page available
10.1096/fasebj.2019.33.1_supplement.82.2
Neutral lipids are a critical source for cellular energy and are stored within specialized organelles known as lipid droplets (LD). Degradation of LDs for energy utilization is accomplished by two principal pathways: lipolysis that is activated by cAMP to recruit adipose triglyceride lipase (ATGL) to the LD surface, and lipophagy that utilizes the autophagic machinery to target and traffic LDs for degradation by lysosomal acid lipase (LAL). However, the mechanisms underlying synergy between these seemingly distinct pathways are not well understood. Previous studies show that autpohagic membrane cannot effectively engulf large organelles, but is size‐restricted to small cargo. Based on this, we HYPOTHESIZE that lipolysis and lipophagy are sequential pathways whereby lipolysis first reduces the size of large LDs to allow for subsequent autophagic engulfment of small LDs for lipophagy. Methods Using light and electron microscopy combined with biochemical approaches, we explored LD size and the sequential nature of lipolysis and lipophagy in primary rat and AML12 hepatocytes. Live‐cell microscopy was used for the first time to monitor LDs transitioning from lipolysis in the cytoplasm to lipophagy within endolysosomal vesicles. Results Confocal microscopy of endogenous ATGL revealed a preferential association with large LDs with an average size of 4.0 μm 2 , seven‐fold larger than LDs not associated with ATGL. In striking comparison, LDs associated with components of the autophagic machinery (LC3, Lamp3) were 50% smaller in size (0.39 μm 2 ). Consistent with this observation, siRNA knockdown of ATGL resulted in the persistence of large LDs (2.8 μm 2 ), whereas knockdown of LAL left cells filled with numerous small LDs (1.5 μm 2 ). These observations were mimicked by inhibitors of ATGL (atglistatin) and LAL (lalistat). In support of these findings, differential centrifugation of AML12 homogenates allowed for separation of two distinct populations of LDs: a buoyant fraction of large LDs enriched in the cytosolic lipase ATGL, and a second collection of smaller, less buoyant LDs enriched in lysosomal enzymes such as Lamp2A, the autophagosome marker LC3‐II, and the endosomal marker Tsg101. Most interesting are time lapse movies of live cells showing engulfment of small LDs by a Lamp3‐positive late endosomal compartment, suggesting that these organelles play an important role in the direct targeting and engulfment of LDs for lipophagy. Conclusion Hepatocytes appear to catabolize LDs in a tandem stepwise process that first utilizes cytosolic lipases to substantially reduce LD size, thereby allowing for subsequent engulfment of small LDs by autophagosomes as well as late endosomes and lysosomes. Support or Funding Information Supported by NIAAA RO1AA020735 to MAM; NIDDK award T32DK007352 to MBS and RJS, and the Mayo Clinic Kogod Aging Fellowship to MBS. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .
Lipid Droplet Size Determines Cooperation of Lipolysis and Lipophagy in Hepatocytes.
Weller, Shaun G. , McNiven, Mark A. , Schott, Micah B. , Schulze, Ryan J.
The FASEB Journal | June 21, 2021 | Volume: 32 | Issue: S1 | Pages: No page available
10.1096/fasebj.2018.32.1_supplement.539.16
Fatty liver disease affects 80–100 million Americans and is a precursor to irreversible and sometimes fatal liver damage. The initial stages of fatty liver disease are marked by the hepatocellular accumulation of fat‐storage organelles known as lipid droplets (LDs) that are degraded by two pathways: lipolysis that involves the recruitment of cytosolic lipases (ATGL, HSL) to the LD surface, and lipophagy that relies on autophagic membranes to target and traffic LDs for lysosomal degradation. Importantly, the mechanisms underlying a cooperation between these seemingly distinct pathways are not well understood. Previous studies have shown that the autophagic engulfment of cytosolic cargo is size‐restricted. Because of this, we HYPOTHESIZE that lipolysis and lipophagy occur as sequential processes initiated by cytosolic lipases to reduce LD size and allow for subsequent engulfment by autophagic membranes. Methods In AML12 hepatocytes, immunofluorescence microscopy and biochemical approaches were used to determine the enrichment of lipolysis vs lipophagy machinery on large vs. small LDs. Live‐cell microscopy was used for the first time to monitor LDs transitioning from lipolysis to lipophagic engulfment. Results Confocal microscopy of AML12 cells immunolabeled for adipose triglyceride lipase (ATGL) revealed a preferential association with large LDs with an average area of 4.0 μm 2 , seven‐fold larger than LDs not associated with ATGL. In striking comparison, LDs associated with components of the autophagic machinery (LC3) were two‐fold smaller in area (0.39 μm 2 ). Consistent with this observation was the finding that siRNA knockdown of ATGL resulted in the persistence of large LDs (2.8 μm 2 ), whereas knockdown of lysosomal acid lipase (LAL) left cells filled with many LDs of a smaller size (1.5 μm 2 ). These observations were mimicked by inhibitors of ATGL (atglistatin) and lysosomal acidification (chloroquine). In support of these findings, differential centrifugation of AML12 homogenates allowed for separation of two distinct populations of LDs: a buoyant fraction of large LDs enriched in the cytosolic lipase ATGL, and a second collection of smaller, less buoyant LDs enriched in lysosomal enzymes such as Lamp2A and the autophagosome marker LC3‐II. Most interesting are time lapse movies of live cells showing engulfment of small LDs by a LAMP3‐positive late endosomal/lysosomal compartment, suggesting that these organelles play an important role in the direct targeting and engulfment of LDs for lipophagy. Conclusion Hepatocytes appear to catabolize LDs in a tandem stepwise process that first utilizes cytosolic lipases to substantially reduce LD size, thereby allowing for subsequent engulfment by autophagosomes as well as late endosomes and lysosomes. Support or Funding Information This study was generously supported by funding from NIAAA R01AA020735, NIDDK T32DK007352, and the Mayo Clinic Robert and Arlene Kogod Center on Aging. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1
Klionsky, Daniel J., Abdel‐Aziz, Amal Kamal , Abdellatif, Mahmoud , Abdoli, Asghar , Abel, Steffen , Abeliovich, Hagai , Abildgaard, Marie H. , Abudu, Yakubu Princely , Acevedo‐Arozena, Abraham , Adamopoulos, Iannis E. , Adeli, Khosrow , Adolph, Timon E. , Adornetto, Annagrazia , Aflaki, Elma, Agam, Galila , Aggarwal, Bharat B. , Agnello, Maria, Agostinis, Patrizia , Agrewala, Javed N. , Agrotis, Alexander , Aguilar, Patricia V., Ahmad, S. Tariq, Ahumada-Castro, Ulises , Aits, Sonja , Aizawa, Shu, Akkoç, Yunus , Akoumianaki, Tonia, Akpinar, Hafize Aysin , Al‐Abd, Ahmed M. , Al-Akra, Lina, Gharaibeh, Abeer , Alaoui‐Jamali, Moulay A. , Alberti, Simon , Alessandri, Cristiano , Alonso, Alicia , Altan‐Bonnet, Nihal , Álvarez, Élida, Alves, Sara , Costa, Cristine Alvès da , Alzaharna, Mazen M. , Amadio, Marialaura , Amantini, Consuelo , Amaral, Cristina , Ambrosio, Susanna , Amer, Amal O. , Ammanathan, Veena , An, Zhenyi, Andrabi, Shaida A. , Andres, Allen M. , Ann, David K. , Anozie, Uche C. , Ansari, Mohammad Y. , Antas, Pedro , Antebi, Adam , Antón, Zuriñe , Anwar, Tahira , Apétoh, Lionel , Araki, Toshiyuki , Araki, Yasuhiro , Araya, Jun , Arévalo, María‐Ángeles , Argüelles, Sandro , Arias, Esperanza , Arikkath, Jyothi , Ariosa, Aileen, Aroca, Ángeles , Arroyo, Daniela S., Arsov, Ivica, Artero, Rubén , Asaro, Dalia Maria Lucia, Ashur‐Fabian, Osnat , Atanasov, Atanas G. , Au, Alicia K. , Auberger, Patrick , Auner, Holger W. , Aurelian, Laure , Avagliano, Laura , Ávalos, Yenniffer , Aveleira, Célia A. , Aydın, Yücel , Ayyadevara, Srinivas , Azzopardi, Maria , Baba, Misuzu, Backer, Jonathan , Bae, Soo Han , Baehrecke, Eric H. , Bagetta, Giacinto , Bagniewska‐Zadworna, Agnieszka , Bai, Hua , Bai, Xiyuan , Bairagi, Nandadulal , Baksi, Shounak , Balbi, Teresa , Ballester, María , Balazadeh, Salma , Balzan, Rena , Bandopadhyay, Rina , Banerjee, Sulagna , Bánréti, Ágnes , Baracca, Alessandra , Barbati, Cristiana , Bargiela, Ariadna , Barilà, Daniela , Barlow, Peter G. , Barmada, Sami J. , Barreiro, Esther , Bártek, Jiří , Bartel, Bonnie , Bartolomé, Alberto , Barve, Gaurav , Bassham, Diane C. , Baulieu, E.E. , Baumgarner, Bradley L. , Bayry, Jagadeesh , Beale, Rupert , Beau, Isabelle , Beaumatin, Florian , Bechara, Luiz Roberto Grassmann , Beck, George R. , Beers, Michael F. , Begun, Jakob , Behrends, Christian , Bejarano, Eloy , Bel, Shai , Belaïd, Amine , Belgareh‐Touzé, Naïma, Bellarosa, Cristina , Belleudi, Francesca , Belló-Pérez, Melissa , Beltran, Jackeline Soares de Oliveira , Beltran, Sebastián, Benbrook, Doris M. , Bendorius, Mykolas , Benítez, Bruno A. , Benito‐Cuesta, Irene , Bensalem, Julien , Berchtold, Martin W. , Berezowska, Sabina , Bergamaschi, Daniele , Berliocchi, Laura , Berlioz‐Torrent, Clarisse , Bernard, Amélie , Besirli, Cagri G. , Besteiro, Sébastien , Betin, Virginie M.S., Beyaert, Rudi , Bezbradica, Jelena S. , Bhaskar, Kiran , Bhatia‐Kiššová, Ingrid, Bhattacharya, Sujoy , Bhuiyan, Md. Shenuarin , Bi, Xiaolin , Biden, Trevor J. , Bijian, Krikor , Billes, Viktor , Binart, Nadine , Bincoletto, Cláudia , Blanco, Gonzalo , Blas‐García, Ana , Błasiak, Janusz , Blomgran, Robert , Blum, Janice S. , Boada-Romero, Emilio, Boban, Mirta , Boeuf, Philippe , Boland, Barry , Bomont, Pascale , Bonaldo, Paolo , Bonam, Srinivasa Reddy , Bonfili, Laura , Bootman, Martin D. , Bordi, Matteo , Borner, Christoph , Bornhäuser, Beat , Bose, Santanu , Botas, Juan , Boulanger, Chantal M. , Bourgeois, Benjamin , Bourke, Nollaig M. , Bousquet, Guilhem , Boya, Patricia , Bozhkov, Peter V. , Bozi, Luiz H. M. , Bozkurt, Tolga O. , Pedro, José Manuel Bravo‐San , Brest, Patrick , Bringer, Marie-Agnès , Briones‐Herrera, Alfredo , Broaddus, V. Courtney, Brodersen, Peter , Brodsky, Jeffrey L. , Bronson, Paola G. , Bronstein, Jeff M. , Brown, Rhoderick E. , Brum, Patrı́cia C. , Bruno, Daniele , Bryson‐Richardson, Robert J. , Bucci, Cecilia , Buchrieser, Carmen , Bueno, Marta , Buchan, J. Ross , Buckingham, Erin M., Budak, Hikmet , Budini, Mauricio , Bultynck, Geert , Burada, Florin , Burgoyne, Joseph R. , Burón, María I. , Bustos, Victor , Büttner, Sabrina , Byrd, Aaron , Cabas, Isabel , Cabrera, Sandra , Cadwell, Ken , Cai, Jingjing , Cai, Lu , Cai, Qian , Calbet, José A. L. , Caldwell, Guy A. , Call, Jarrod A. , Calvani, Riccardo , Calvo, Ana Cristina , Calvo‐Rubio, Miguel , Câmara, Niels Olsen Saraiva , Camonis, Jacques , Camougrand, Nadine , Campanella, Michelangelo , Campbell, Edward M. , Campos, Juliane C. , Camuzard, Olivier , Cancino, Jorge , Caniggia, Isabella , Canonico, Barbara , Cantı́, Carles , Cao, Bin , Caramés, B. , Cardenal‐Muñoz, Elena , Cárdenas, César , Cárdenas, Luis , Cardoso, Sandra M. , Carew, Jennifer S. , Carle, Georges F. , Carleton, Gillian , Carloni, Silvia , Carneiro, Letícia A. M. , Carosi, Julian M. , Carra, Serena , Carrier, Alice , Carter, A. Brent, Carvalho, Andreia Neves , Casanova, Magali , Casas, Josefina , Cassioli, Chiara , Castillo, Karen , Castillo‐Lluva, Sonia , Castoldi, Francesca , Castori, Marco , Castro, Ariel F. , Castro‐Hernández, Javier , Cavadas, Cláudia , Cavaliere, Federica, Cavallini, Gabriella , Cavinato, Maria , Rica, Paula Cebollada , Cechowska‐Pasko, Marzanna , Cerqueira, João , Cerutti, Janete M. , Çetintaş, Vildan Bozok , Cetrullo, Silvia , Chagin, Andrei S. , Chai, Chee‐Yin , Chakrabarti, Gopal , Chakraborty, Tapas , Chakraborty, Trinad , Chami, Mounia , Chamilos, Georgios , Chan, David W. , Chan, Edmond Y. W., Chan, Ho Yin Edwin , Chan, Helen H., Chan, Hung , Chan, Matthew T.V. , Chan, Yau Sang , Chang, Hao‐Chun , Chang, Kai , Chao, Jie , Charlet‐Berguerand, Nicolas , Chatterjee, Samrat , Chaube, Shail K. , Chaudhary, Anu , Chauhan, Santosh , Chaum, Edward , Checler, Frédéric , Cheetham, Michael E. , Chen, Chang‐Shi , Chen, Jian‐Fu , Chen, Liam L., Chen, Mingliang , Chen, Mu‐Kuan , Chen, Ning , Chen, Wei , Chen, Xinming , Chen, Xiongwen , Chen, Yan , Chen, Ye‐Guang , Chen, Yingyu , Chen, Yongqiang , Chen, Zhefan Stephen , Chen, Zhihua , Cheng, Xiu‐Tang , Cheng, Yiyun , Cheng, Zhiyong , Cheong, Jit Kong , Cherry, Sara , Cheung, Chi F., Cheung, Chun Hei Antonio , Cheung, King‐Ho , Chevet, Éric , Chi, Richard J., Chiaradonna, Ferdinando , Chiariello, M , Chica, Nathalia , Chiocca, Susanna , Chiong, Mario , Chiou, Shih‐Hwa , Chiramel, Abhilash I., Chiurchiù, Valerio , Cho, Dong-Hyung, Choe, Seong‐Kyu , Choi, Augustine M.K. , Choi, Mary E. , Choudhury, Kamalika Roy , Chow, Norman , Chua, Jason P. , Chua, John Jia En , Chung, Hyewon , Chung, Kin Pan , Chung, So‐Hyang , Chung, Yuen-Li, Ciechomska, Iwona A. , Cinque, Laura , Çırak, Sebahattin , Clarke, Robert , Clementi, Emilio , Coccia, Eliana M. , Codogno, Patrice , Colasanti, Tania , Colasuonno, Fiorella , Colbert, Robert A. , Colell, Anna , Coll, Núria S. , Collins, Mark O. , Colombo, Marı́a I. , Colón‐Ramos, Daniel A. , Cominetti, Márcia R. , Consiglio, Antonella , Conte, A. , Contu, Viorica Raluca , Cookson, Mark , Coombs, Kevin M. , Costa, Maria do Carmo , Costantino, Sarah , Costelli, Paola , Criollo, Alfredo , Crippa, V. , Cristofani, Riccardo , Csizmadia, Tamás , Cui, Bing , Cui, Yixian , Culetto, Emmanuel , Cumino, Andrea C. , Cybulsky, Andrey V. , Czaja, Mark J. , Czuczwar, Stanisław J. , D’Adamo, Stefania , D’Amelio, Marcello , D’Orazi, Gabriella , Silva, James Almada da , Dafsari, Hormos Salimi , Daglia, Maria , Dai, Xiaoxia , Dai, Yun , Dai, Yuyuan , Col, Jessica Dal , Dalhaimer, Paul , Valle, Luisa Dalla , Dallenga, Tobias , Dalmasso, Guillaume , Dando, Ilaria , Das, Hiranmoy , Dasari, Santosh K. , Dash, Srikanta, Dauphinee, Adrian N. , Davies, Jeffrey S. , Dávila, Valeria A. , Davis, Roger J. , Naidu, Sharadha Dayalan , Bosscher, Karolien De , Leonibus, Chiara De , Barbosa, Mayara Garcia de Mattos , Meyer, Guido R.Y. De , Palma, Clara De , Virgilio, Claudio De , Zio, Daniela De , Decuypere, Jean-Paul , Deehan, Mark , Deflorian, Gianluca , Dehay, Benjamin , Delaney, Joe R. , Delorme‐Axford, Elizabeth , Demers, Nicholas D. , Deng, Hongbin , Dengjel, Jörn , Dent, Paul, DePamphilis, Melvin L., Descoteaux, Albert , Devis, Laura , Devkota, Sushil , Devuyst, Olivier , Dewson, Grant , Dharmasivam, Mahendiran , Domenico, Fabio Di , Fazio, Pietro Di , Fonzo, Alessio Di , Guardo, Giovanni Di , Guglielmo, Gianni M. Di , Leo, Luca Di , Malta, Chiara Di , Nardo, Alessia Di, Rienzo, Martina Di , Diao, Jiajie , Diaz-Araya, Guillermo, Díaz‐Laviada, Inés , Dickinson, Jared M. , Diederich, Marc , Dieudé, Mélanie , Ding, Shiping , Ding, Wen-Xing, Dinić, Jelena , Dinić, Miroslav , Dinkova‐Kostova, Albena T. , Distler, Jörg H. W. , Đokić, Jelena , Emre, Serap , Dong, Xiaonan , Dong, Zhiwu , Dorn, Gerald W. , Dou, Juan, Dowaidar, Moataz , Drucker, Liat , Du, Ailian , Du, Guangwei , Du, Hai‐Ning , Toit, André du , Duan, Shao-Bin , Duan, Xiaoqiong , Duarte, Sónia , Dupont, Nicolas , Durán, Raúl V. , Dyshlovoy, Sergey A. , Ebrahimi‐Fakhari, Darius , Eckhart, Leopold , Edelstein, Charles L. , Efferth, Thomas , Eid, Nabil , Eisenberg, Tobias , Eissa, N. Tony, Ejarque, Miriam , Andaloussi, Abdeljabar El, El‐Hage, Nazira , Eleuteri, Anna Maria , El‐Shafey, Eman S. , Elgendy, Mohamed , Elizalde, María Mercedes , Elsässer, Hans‐Peter , Elsherbiny, Eslam S. , Emre, N. C. Tolga , Eng, Christina H. , Engedal, Nikolai , Engelsen, Agnete S. T. , Enserink, Jorrit M. , Escalante, Ricardo , Esclatine, Audrey , Eskelinen, Eeva‐Liisa , Espert, Lucile , Eusebio, Makandjou-Ola , Facchiano, Antonio , Facchiano, Francesco , Fadeel, Bengt , Fader, Claudio M., Faesen, Alex C. , Fairlie, W. 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H. , Ma, Ning-Fang, Ma, Quanhong , Ma, Xinliang , Ma, Yueyun , Ma, Zhenyi , MacDougald, Ormond A. , MacIntosh, Gustavo C. , Macleod, Kay F. , Maday, Sandra , Madeo, Frank , Madesh, Muniswamy , Madl, Tobias , Madrigal‐Matute, Julio , Maeda, Akiko, Maejima, Yasuhiro , Magariños, Marta , Mahavadi, Poornima , Maiani, Emiliano , Maiese, Kenneth , Maiti, Panchanan , Maiuri, Maria Chiara , Major, Michael Ben, Makareeva, Elena , Malik, Fayaz , Mallilankaraman, Karthik , Maloyan, Alina , Mammadova, Najiba, Man, Gene Chi Wai , Manai, Federico , Mancias, Joseph D. , Mandelkow, Eva‐Maria , Manfredi, Angelo A. , Manshian, Bella B. , Manzano, Raquel , Marchese, Chiara , Marchetti, Sandrine , Marcucci, F, Mardente, Stefania , Mareninova, Olga A. , Mari, Muriel , Marinelli, Sara , Mariño, Guillermo , Mariotto, Sofia , Martin, Alexandre , Martin, Katie R. , Martin, Sara L. , Martín‐Segura, Adrián , Martin-Burriel, Inmaculada, Martín-Rincón, Marcos , Martín‐Sanz, Paloma , Martinez, Aitor , Martı́nez, Ana , Martinez-Lopez, Nuria, Martínez‐Vicente, Marta , Martins, Daniel Oliveira , Martins, Joilson O. , Martins, Waleska K. , Martins-Marques, Tania, Marzetti, Emanuele , Masaldan, Shashank , Masclaux-Daubresse, Celine, Mashek, Douglas G. , Massa, Valentina , Massieu, Lourdes , Masyuk, Anatoliy I. , Masyuk, Tetyana V., Matheu, Ander , Matoba, Satoaki , Matsuzaki, Sachiko , Mattar, Pamela , Mattè, Alessandro , Mauriz, José L., Mauthe, Mario , Maycotte, Paola , Mayer, Johanna , Mazzoni, Cristina , Mazzulli, Joseph R. , McCarty, Nami , McGill, Mitchell R. , McKenna, Sharon L. , McLoughlin, Fionn , McNiven, Mark A., McWilliams, Thomas G. , Medeiros, Tania , Medina, Diego L., Megeney, Lynn A. , Megyeri, Klára , Mehrpour, Maryam , Mehta, Jawahar L. , Meijer, Alfred J., Mejlvang, Jakob , Meléndez, Alicia , Melk, Annette, Memişoğlu, Gönen , Mendes, A.F. , Meng, Delong , Meng, Fei, Mercier, A., Mergny, Jean‐Louis , Merkley, Seth D. , Meske, Volker, Mestre, Ana Cecilia, Metur, Shree Padma, Meyer, C., Meyer, Hemmo , Mi, Wenyi , Mialet‐Perez, Jeanne , Miao, Jun‐Ying, Micale, Lucia , Miki, Yasuo, Milan, Enrico , Milczarek, Małgorzata , Miller, Samuel I. , Millward, Steven W. , Mirzaei, Hamed, Mirzaei, Hamid Reza , Mirzaei, Mehdi , Mishra, Amit , Mishra, Nandita , Mishra, Paras Kumar, Misirkić, Maja , Misasi, Roberta, Misra, Amit , Misso, Gabriella , Mitchell, Claire H. , Mitou, Géraldine, Miura, Tetsuji , Miyazaki, Makoto, Miyazaki, Mitsunori , Miyazaki, Taiga , Miyazawa, Keisuke, Mizushima, Noboru , Mogensen, Trine H. , Mohammadinejad, Reza , Mohamud, Yasir , Mohanty, Abhishek , Möhlmann, Torsten , Moley, Kelle H. , Möller, Andreas, Mollereau, Bertrand , Mollinedo, Faustino, Montagna, Costanza , Monteiro, Mervyn J. , Montella, Andrea , Montes, L. Ruth , Montico, Barbara , Mony, Vinod K., Compagnoni, Giacomo Monzio , Moore, Michael N. , Moosavi, Mohammad Amin , Morales‐Álamo, David , Moratalla, Rosario , Moreira, Paula I. , Morelli, Elena , Moreno-Blas, Daniel , Morgan, Alwena H. , Morin, Fabrice , Morishita, Hideaki , Moriyama, Mariko , Moriyasu, Yuji, Morleo, Manuela , Morselli, Eugenia , Moruno-Manchon, Jose F. , Moscat, Jorge , Motori, Elisa , Moura, Andréa Felinto , Mrakovcic, Maria, Muciño-Hernández, Gabriel, Mukherjee, Anupam , Mukhopadhyay, Subhadip , Levy, Jean M. Mulcahy , Mulero, Victoriano, Muller, Sylviane, Münch, Christian , Muñoz-Cánoves, Pura, Muñoz‐Galdeano, Teresa , Murakawa, Tomokazu , Murphy, Brona M. , Murthy, Aditya, Myöhänen, Timo T. , Mysorekar, Indira U. , Mytych, Jennifer , Nabavi, Seyed Mohammad , Nagy, Péter , Nahimana, Aimable , Nakagawa, Ichiro, Nakamura, Ken , Nandi, Shyam Sundar , Nanjundan, Meera, Nanni, Monica , Napolitano, Gennaro , Narita, Masashi, Nassif, Melissa , Nathan, Ilana , Natsumeda, Manabu , Naudé, Ryno J., Naumann, Christin , Naveiras, Olaia , Navid, Fatemeh , Nawrocki, Steffan T., Nazarko, Taras Y. , Nazio, Francesca , Negoita, Florentina , Neill, Thomas , Neisch, Amanda L. , Netea, Mihai G. , Neubert, Patrick , Neumann, Dietbert , Neutzner, Albert , Newton, Phillip T. , Ney, Paul A., Ng, Charlene Cheuk Wing, Ng, T.B., Nguyen, Hang Thi Thu , Nguyen, Long T. , Ni, Hong-Min, Cheallaigh, Clíona Ní , Ni, Zhenhong , Nicolao, M. Celeste, Nicoli, Francesco , Nieto‐Díaz, Manuel , Niranjan, Rituraj , Nishimune, Hiroshi , Niso-Santano, Mireia, Nixon, Ralph A. , Nobili, Annalisa , Noda, Takeshi , Nogueira-Recalde, Uxía , Nombela, Iván , Novak, Ivana, Novoa, Beatriz , Nukina, Nobuyuki , Nussbaum-Krammer, Carmen, Nylandsted, Jesper , O’Donovan, Tracey R. , O’Leary, Seónadh M. , O’Rourke, Eyleen J. , O’Sullivan, Mary P. , O’Sullivan, Timothy E., Oddo, Salvatore , Oehme, Ina, Ogawa, Michinaga , Ogier‐Denis, Éric , Ögmundsdóttir, Margrét H. , Öğretmen, Besim , Oh, Goo Taeg , Oh, Seon‐Hee , Oh, Young J. , Ohama, Takashi, Ohashi, Yohei , Ohmuraya, Masaki, Oikonomou, Vasileios , Ojha, Rani , Okazawa, Hitoshi , Oku, M., Oliván, Sara , Oliveira, Jorge M.A. , Ollmann, Michael, Olzmann, James A. , Omari, Shakib , Önal, Gizem, Ondrej, Martin , Ong, Sang‐Bing , Onnis, Anna , Orellana, Juan , Orellana‐Muñoz, Sara , Ortega-Villaizán, María del Mar , Ortiz‐González, Xilma R. , Osiewacz, Heinz D. , Osman, Abdel‐Hamid K. , Otsu, Kinya, Ott, Christiane , Ou, Jing-hsiung James, Outeiro, Tiago F., Öztürk, Melek , Pagès, Gilles, Pahari, Susanta , Pajares, Marta, Pal, Rituraj, Paladino, Simona , Palmieri, Michela , Palmisano, Giuseppe , Pan, Qingjun , Pan, Xin , Panasyuk, Ganna , Pandey, Rahul , Pandey, Udai B., Pandya, Vrajesh , Paneni, Francesco , Pang, Shirley Yin-Yu, Papademetrio, Daniela L. , Papinski, Daniel, Papp, Diana , Park, Hwan Tae , Park, Ji-Man, Park, Jong‐In , Park, Junsoo, Park, Sang-Youel, Pasquier, Adrien , Pasquier, Benoit , Passos, João F. , Pastore, Nunzia , Patschan, Daniel , Pattingre, Sophie , Pedraza‐Alva, Gustavo , Pedraza-Chaverri, Jose, Pedrozo, Zully , Pei, Gang , Pei, Jianming , Peled-Zehavi, Hadas, Pellegrini, Joaquín Miguel , Pelletier, Joffrey , Peñalva, Miguel A., Peng, Di , Peng, Ying , Pennuto, Maria , Pentimalli, Francesca , Pereira, Cláudia MF, Pereira, Gustavo J.S. , Pereira, Lílian Cristina , Almeida, Luís Pereira de , Perera, Nirma D. , Pérez-Lara, Ángel, Pérez‐Oliva, Ana B. , Perl, András , Pestell, Richard G. , Petrache, I., Petrovski, Goran , Pfirrmann, Thorsten , Pfister, Astrid S., Pi, Huifeng , Pickrell, Alicia M. , Picot, Sandy, Pierantoni, Giovanna Maria , Pierre, Philippe , Pierrefite‐Carle, Valérie , Pierzynowska, Karolina , Pietruczuk, Mirosława , Pimentel-Muiños, Felipe X., Pinar, Mario , Pinheiro, Roberta Olmo , Pinkas‐Kramarski, Ronit , Pircs, Karolina , Piya, Sujan , Pizzo, Paola , Platta, Harald W. , Plomann, Markus , Pocock, Roger , Pöggeler, Stefanie , Pohl, Christian, Poirot, Marc , Poletti, Angelo , Ponpuak, Marisa , Popelka, Hana , Popova, Bilyana , Porta, Helena, Alcón, Soledad Porte , Portilla-Fernández, Eliana , Potts, Malia B. , Powers, Ted, Prahlad, Veena , Prajsnar, Tomasz K. , Praticò, Domenico , Prencipe, Rosaria, Priault, Muriel , Proikas‐Cezanne, Tassula , Puertollano, Rosa , Puglielli, Luigi, Pulinilkunnil, Thomas , Puri, Deepika , Puri, Rajat, Puyal, Julien , Qi, Yongmei , Quadrilatero, Joe , Quarleri, Jorge, Raben, Nina, Rabinowich, Hannah, Ragona, Debora, Rahmati, Marveh , Raia, Valeria, Raimundo, Nuno , Rajasekaran, Namakkal-Soorappan, Rao, Sriganesh Ramachandra , Rami, Abdelhaq, Ramírez‐Pardo, Ignacio , Ramsden, D. , Randow, Felix , Ranieri, Danilo , Rao, Hai , Rao, Rekha , Rathore, Sumit , Ratnayaka, J. Arjuna , Ratovitski, Edward A., Ravanan, Palaniyandi, Ravegnini, Gloria , Ray, Swapan K. , Rebecca, Vito, Reggiori, Fulvio , Reigada, David , Reiling, Jan H., Rein, Theo , Reipert, Siegfried , Rekha, Rokeya Sultana , Ren, Hongmei, Ren, Jun , Ren, Weichao , Renault, Tristan, Renga, Giorgia , Reue, Karen, Rewitz, Kim , Ramos, Bruna Ribeiro de Andrade , Riazuddin, S. Amer, Ribeiro‐Rodrigues, Teresa , Riccio, Victoria , Richardson, Des R. , Risbud, Makarand V. , Risueño, Ruth M. , Ritis, Konstantinos, Rizza, Salvatore , Rizzuto, Rosario , Roberts, Scott J. , Roberts, Luke D., Robinson, Katherine J. , Rocchi, Stéphane , Rodrigues, Tiago , Silva, Vagner Ramon Rodrigues , Rodriguez-Barrueco, Ruth, Rodríguez‐Henche, Nieves , Rogers, Robert S. , Rogov, Vladimir V., Rojo, Ana I. , Romanello, Vanina, Romani, Luigina , Romano, Alessandra , Romano, Patricia Silvia , Romeo-Guitart, David, Romero, Luís C. , Romero, Montserrat , Roney, Joseph C. , Rongo, Christopher , Rosenfeldt, Mathias T. , Rosenstiel, Philip , Rosenwald, Anne , Roth, Steven, Rouschop, Kasper M.A. , Roussel, Benoit D. , Roux, Sophie , Rovere–Querini, Patrizia, Roy, Ajit , Rozières, Aurore , Ruano, Diego , Rubtsova, Maria P. , Ruckdeschel, Klaus, Ruckenstuhl, Christoph , Rudolf, Emil, Rudolf, Rüdiger, Ruggieri, Alessandra , Ruparelia, Avnika A. , Rusmini, P. , Russell, Ryan R., Russo, Gian Luigi , Russo, Maria , Russo, Rossella , Ryabaya, O. O. , Sabater-Arcis, María , Sacher, M, Sachse, Carsten , Sadhu, Abhishek , Säftig, Paul , Sahebkar, Amirhossein, Şahin, Mustafa , Şahin, Özgür , Saito, Nayuta , Saito, Tsunenori , Sakai, Yasuyoshi , Sakamaki, Jun-Ichi , Saksela, Kalle , Salazar, Gloria , Salazar-Degracia, Anna, Salekdeh, Ghasem Hosseini , Saluja, Ashok K. , Sampaio‐Marques, Belém , Sánchez, Marı́a C. , Sánchez-Alcázar, José A., Sanchez‐Vera, Victoria , Sancho‐Shimizu, Vanessa , Santambrogio, Laura , Santana, Magda M., Santoni, G, Sanz, Alberto , Saran, Shweta , Sardiello, Marco, Sargeant, Timothy J. , Sarin, Apurva , Sarkar, Chinmoy, Sarkar, Sovan , Sarrias, Maria-Rosa, Sarkar, Surajit , Sarmah, Dipanka Tanu, Sarparanta, J. , Sathyanarayan, Aishwarya , Ranganayaki, S. , Scaglione, K. Matthew , Scatozza, Francesca , Schafer, Zachary T. , Schaible, Ulrich E., Schapira, Anthony H.V. , Scharl, Michael , Schein, Catherine H. , Schiaffino, Maria Vittoria , Schiappacassi, Mónica , Schindl, Rainer , Schlattner, Uwe , Schmidt, Oliver, Schmitt, Roland , Schmidt, Stephen D., Schmitz, Ingo , Schmukler, Eran, Schneider, Anja , Schneider, Bianca E. , Schober, Romana , Schoijet, Alejandra C. , Schramm, M., Schröder, Bernd , Schuh, Kai , Schüller, Christoph , Schulze, Ryan J. , Schürmanns, Lea , Schwamborn, Jens C. , Schwarten, Melanie , Scott, Melanie J. , Scotto, Kathleen W., Scrima, Andrea , Scrivo, Aurora , Sebastián, David , Sebti, Salwa , Sedej, Simon , Segev, Nava , Seglen, Per O., Selleck, Scott B. , Selsby, Joshua, Sendtner, Michael , Şentürk, Şerif , Seranova, Elena, Sergi, Consolato M., Serra-Moreno, Ruth , Sesaki, Hiromi , Settembre, Carmine, Setty, Subba Rao Gangi , Sgarbi, Gianluca , Sha, Ou , Shacka, John J., Shah, Javeed A. , Shang, Dantong, Shao, Feng, Sharbati, Soroush , Sharkey, Lisa M. , Sharma, Dipali , Sharma, Gaurav, Sharma, Kulbhushan , Sharma, Pawan , Sharma, Surendra, Shen, Han‐Ming , Shen, Hongtao , Shen, Jiangang , Shen, Ming , Shen, Weili , Shen, Zheni, Sheng, Rui , Sheng, Zu-Hang, Shi, Jianjian , Shi, Ying–Hong , Shiba‐Fukushima, Kahori, Shieh, Jeng‐Jer , Shimada, Yohta , Shimizu, Shigeomi, Shimozawa, Makoto , Shintani, Takahiro , Shoemaker, Christopher J. , Shojaei, Shahla, Shoji, Ikuo , Shravage, Bhupendra V. , Shridhar, Viji, Shu, Chih‐Wen , Shu, Hong-Bing, Shui, Ke, Shukla, Arvind Kumar , Shutt, Timothy E. , Sica, Valentina , Siddiqui, Aleem , Sierra-Torre, Virginia, Signorelli, Santiago , Silva, Bruno Jorge de Andrade , Silva, Johnatas D. , Silva-Pavez, Eduardo , Silvente‐Poirot, Sandrine , Simmonds, Rachel E. , Singh, Anurag K. , Singh, Rajat Kumar , Singh, Shivendra V. , Singh, Shrawan Kumar , Singh, Sudha , Singh, Sunaina , Singh, Surinder Pal , Sinha, Debasish, Sinha, Rohit A. , Sinha, Sangita, Sirko, Agnieszka , Sivridis, Efthimios L., Skendros, Panagiotis , Sohn, Eun Jung , Sok, Sophia P. 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David , Sze, Stephen Cho Wing , Szewczyk, Nathaniel J. , Tabęcka-Łonczynska, Anna, Tabolacci, Claudio , Taegtmeyer, Heinrich, Tagaya, Mitsuo , Tai, Haoran , Tait, Stephen W. G., Takahashi, Yoshinori , Tam, Chit , Tam, Shing Yau , Tampellini, Davide , Tamura, Atsushi , Tan, Eng-King, Tan, Ya‐Qin , Tanaka, Masaki , Tang, Daolin , Tang, Jingfeng , Tang, Tie-Shan , Tao, Zhipeng , Taouis, Mohammed , Tavernarakis, Nektarios, Taylor, Allen, Teixeira, Natércia , Tekirdağ, Kumsal Ayşe, Tencomnao, Tewin , Tenreiro, Sandra , Tharaux, Pierre‐Louis , Thedieck, Kathrin , Thekkinghat, Arvind A. , Thinwa, Josephine , Thirumalaikumar, Venkatesh P. , Thomes, Paul G. , Thorburn, Andrew , Thum, Thomas, Thumm, Michael , Tian, Ling, Tichý, Aleš , Timmerman, Vincent , Titorenko, Vladimir I. , Toivonen, Janne M. , Tomaipitinca, Luana , Tomar, Dhanendra , Tomás‐Zapico, Cristina , Tomić, Sergej , Tong, Chao, Tong, Xin , Torgersen, Maria L., Torii, Satoru , Torres-López, Liliana , Torriglia, Alicia , Towers, Christina G. , Towns, Roberto, Tran, Quynh‐Giao , Travassos, Leonardo H. , Tremel, Shirley , Trougakos, Ioannis P., Tsao, Betty P. , Tse, Tak Fu, Tsvetkov, Andrey S. , Tumbarello, David A. , Tyler, Jessica K., Tyutereva, Elena V. , Uchiyama, Yasuo , Ugun‐Klusek, Aslihan , Uhlig, Holm H. , Ułamek-Kozioł, Marzena, Ulasov, Ilya V. , Umekawa, Midori, Ungermann, Christian , Urbe, Sylvie, Uribe-Carretero, Elisabet , Uversky, Vladimir N. , Vaccaro, María I. , Vahsen, Björn F. , Vakifahmetoglu-Norberg, Helin, Valdor, Rut , Valente, Maria João , Valko, Ayelén , Vallée, Richard, Valverde, Ángela M. , Berghe, Greet Van den, Veen, Stijn van der , Kaer, Luc Van , Loosdregt, Jorg van , Wijk, Sjoerd J. L. van , Vandenberghe, Wim , Vanhorebeek, Ilse , Vannier-Santos, Marcos A., Vannini, Nicola , Vanrell, M. Cristina, Vantaggiato, Chiara , Varela‐Nieto, Isabel , Varga, Máté , Vasconcelos, M. Helena , Vats, Somya , Vega-Rubín-de-Celis, Silvia , Velasco, Guillermo , Velázquez, Ariadna P., Vellai, Tibor , Vellenga, Edo , Verdier, Mireille , Verginis, Panayotis , Vergne, Isabelle , Verkade, Paul , Verma, Manish , Verstreken, Patrik , Vervliet, Tim , Vervoorts, Jörg , Víctor, Víctor M., Vidoni, Chiara , Vieira, Otília V. , Vierstra, Richard D., Viganò, Sonia , Vihinen, Helena , Vijayan, Vinoy, Vila, Miquel , Villalba, José M., Villalobo, Antonio , Villarejo‐Zori, Beatriz , Vincent, Olivier , Vindis, Cécile , Viret, Christophe , Vocadlo, David J. , Voitsekhovskaja, Olga V. , Volonté, Cinzia , Volta, Mattia , Vomero, Marta , Haefen, Clarissa von, Vooijs, Marc , Voos, Wolfgang , Vučićević, Ljubica , Waguri, Satoshi , Waite, Kenrick A., Wakatsuki, Shuji , Walker, David W., Walker, Mark J. , Walter, Jochen, Wandosell, Francisco , Wang, Bo , Wang, Chao-Yung, Wang, Chen , Wang, Chenran, Wang, Chenwei , Wang, Cun-Yu, Wang, Fengming, Wang, Han, Wang, Hexiang , Wang, Hong‐Gang , Wang, Jianrong, Wang, Jigang , Wang, Jun-Dong , Wang, Kui , Wang, Lianrong, Wang, Liming , Wang, Maggie Haitian, Wang, Meiqing , Wang, Nanbu , Wang, Pengwei , Wang, Ping , Wang, Ping, Wang, Q., Wang, Qiong , Wang, Wentao , Wang, Xinnan, Wang, Xuejun , Wang, Yan, Wang, Yanchang , Wang, Yanzhuang , Wang, Yihua , Wang, Yu , Wang, Yuqi , Wang, Zhe, Wang, Zhenyu , Wang, Zhouguang , Watanabe, Eizo, Watchon, Maxinne , Wawrzyńska, Anna , Weaver, Timothy E., Węgrzyn, Grzegorz, Wehman, Ann M. , Wei, Huafeng , Wei, Taotao , Wei, Yongjie, Weiergräber, Oliver H. , Weihl, Conrad C., Weindl, Günther , Weiskirchen, Ralf , Wen, Runxia H. , Werner, Antonia, Weykopf, Beatrice , Whitton, J. 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N. , Bei, Roberto , Behl, Christian , Bello‐Morales, Raquel , Beltrán, Sebastián , Bergami, Matteo , Bergmann, Andreas , Berthoux, Lionel , Bhattacharya, Resham , Bhattacharyya, Shalmoli , Bhutia, Sujit Kumar , Bi, Lanrong , Birgisdottir, Åsa Birna , Bjørkøy, Geir , Blomgren, Klas , Boada-Romero, Emilio , Boesze‐Battaglia, Kathleen , Bonifacino, Juan S. , Boone, Brian A. , Borthakur, Gautam , Bosch, Jürgen , Bose, Santanu , Botana, Luis Miguel , Boulton, Michael E. , Bourdenx, Mathieu , Brackney, Doug E. , Brandts, Christian , Braun, Ralf J. , Braus, Gerhard H. , Bravo, Roberto , Brody, Steven L. , Brown, Carolyn Nicole , Brumell, John Hunter , Brunetti‐Pierri, Nicola , Buitrago‐Molina, Laura Elisa , Buraschi, Simone , Buch, Shilpa J. , Butturini, Elena , Cairó, Montserrat , Caldwell, Kim A. , Campbell‐Valois, François‐Xavier , Campello, Silvia , Campesi, Ilaria , Almeida, Danilo Cândido de , Canesi, Laura , Caraglia, Michele , Carchman, Evie H. , Carmona‐Gutiérrez, Didac , Carnevali, Oliana , Carrier, Lucie , Carroll, Bernadette , Carter, A. Brent , Casas, Caty , Castillo, Eliseo F. , Castro‐Caldas, Margarida , Castro‐Obregón, Susana , Catz, Sergio , Cayuela, María Luisa , Cecarini, Valentina , Cecconi, Francesco , Cenci, Simone , Ceperuelo‐Mallafré, Victòria , Cervia, Davide , Chae, Han–Jung , Chakrabarti, Oishee , Chan, Edmond Y. 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Autophagy | March 24, 2021 | Volume: 17 | Issue: 1 | Pages: 1-382
Direct lysosome-based autophagy of lipid droplets in hepatocytes
Schulze, Ryan J. , Krueger, Eugene W. , Weller, Shaun G. , Johnson, Katherine M. , Schott, Micah B. , McNiven, Mark A. , Schott, Micah B , Johnson, Katherine M., Casey, Carol A.
Proceedings of the National Academy of Sciences | December 7, 2020 | Volume: 117 | Issue: 51 | Pages: 32443-32452
Significance Lipid droplets (LDs) are specialized fat-storage organelles that can be used as a fuel source by many types of cells when nutrients are scarce. One mechanism used by hepatocytes (the functional cells of the liver) for the catabolism of these energy reserves is the lysosome-directed process of autophagy. Traditionally, autophagy necessitates the enclosure of cargo within a double-membrane autophagosome before delivery to the lysosome for degradation. Here, we use live-cell and electron microscopy to demonstrate that stable contacts between LDs and lysosomes in hepatocytes can result in the transfer of both proteins and lipids from LDs directly into the lysosome in the absence of an autophagosomal intermediate. These findings reveal a mechanism used for lipid homeostasis in the liver.