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Lecoquierre, Francois

0000-0002-9110-1856

Mayo Clinic

Université de Rouen Normandie, INSERM U12045 and CHU Rouen, Department of Genetics and Reference Center for Developmental Disorders, FHU-G4 Génomique, Rouen, France.

Citations 6

Loss‐of‐Function Variants in CUL3 Cause a Syndromic Neurodevelopmental Disorder
Blackburn, Patrick R. , Herkert, Johanna C. , Rinne, Tuula , Thiffault, Isabelle, Rapp, Michele, Alders, Mariel, Maas, Saskia M. , Gérard, Bénédicte, Smol, Thomas , Vincent‐Delorme, Catherine , Isidor, Bertrand , Joset, Pascal , Husson, Thomas , Guerrot, Anne‐Marie , Bacino, Carlos A. , Macmurdo, Colleen, Thompson, Stephanie S., Faivre, Laurence , Deb, Wallid , Vignard, Virginie , Goldenberg, Alice, Lecoquierre, François , Zech, Michael , Necpál, Ján , Winkelmann, Juliane , Koprušáková, Monika Turčanová , Konstantopoulou, Vassiliki , Younce, John R. , Mighton, Chloe, Fung, Charlotte, Morel, Chantal F. , Barth, Magalie , Krapels, Ingrid P.C. , Schoot, Vyne van der , Bußmann, Cornelia, Wortmann, Saskia B. , Ravelli, Claudia , Keren, Boris , Ziegler, Alban , Hasadsri, Linda , Pichurin, Pavel N. , Klee, Eric W. , Grand, Katheryn , Sanchez‐Lara, Pedro A. , Krüger, Elke , Klinkhammer, Hannah , Tartaglia, Marco , Wang, Tianyun , Prokisch, Holger , Shinawi, Marwan , Brunet, Theresa , Tartaglia, Marco , Wang, Tianyun , Lecoquierre, Francois , Faivre, Laurence , Ebstein, Frédéric , Hsieh, Tzung‐Chien , Motta, Marialetizia , Radio, Francesca Clementina , Cogné, Benjamin , Vincent, Marie , Bachmann‐Gagescu, Ruxandra , Rauch, Anita , Ferrero, Giovanni Battista , Ciolfi, Andrea , Rosenfeld, Jill A. , Mau‐Them, Frédéric Tran , Agrawal, Pankaj B. , Madden, Jill A. , Goldenberg, Alice , Jech, Robert , Shinawi, Marwan , Lerner‐Ellis, Jordan P. , DiTroia, Stephanie P. , Bonneau, Dominique , Stegmann, Alexander P.A. , Mignot, Cyril , Zampino, Giuseppe , Mayr, Johannes A , Feichtinger, René G. , Courtin, Thomas , Bezieau, Stéphane , Krawitz, Peter Michael , Eichler, Evan E , Küry, Sébastien

Annals of Neurology | September 20, 2024 | Volume: 97 | Issue: 1 | Pages: 76-89

10.1002/ana.27077 Get It

ObjectiveDe novo variants in cullin‐3 ubiquitin ligase (CUL3) have been strongly associated with neurodevelopmental disorders (NDDs), but no large case series have been reported so far. Here, we aimed to collect sporadic cases carrying rare variants in CUL3, describe the genotype–phenotype correlation, and investigate the underlying pathogenic mechanism.MethodsGenetic data and detailed clinical records were collected via multicenter collaboration. Dysmorphic facial features were analyzed using GestaltMatcher. Variant effects on CUL3 protein stability were assessed using patient‐derived T‐cells.ResultsWe assembled a cohort of 37 individuals with heterozygous CUL3 variants presenting a syndromic NDD characterized by intellectual disability with or without autistic features. Of these, 35 have loss‐of‐function (LoF) and 2 have missense variants. CUL3 LoF variants in patients may affect protein stability leading to perturbations in protein homeostasis, as evidenced by decreased ubiquitin‐protein conjugates in vitro. Notably, we show that 4E‐BP1 (EIF4EBP1), a prominent substrate of CUL3, fails to be targeted for proteasomal degradation in patient‐derived cells.InterpretationOur study further refines the clinical and mutational spectrum of CUL3‐associated NDDs, expands the spectrum of cullin RING E3 ligase‐associated neuropsychiatric disorders, and suggests haploinsufficiency via LoF variants is the predominant pathogenic mechanism. ANN NEUROL 2025;97:76–89
Germline mutations in a G protein identify signaling cross-talk in T cells
Ham, Hyoungjun , Jing, Huie , Lamborn, Ian T. , Kober, M. , Anderson, David E. , Druey, Kirk M. , Mandl, Judith N. , Isidor, Bertrand , Freeman, Alexandra F. , Ganesan, Sundar , Karsak, Meliha , Mustillo, Peter , Teo, Juliana , Zolkipli‐Cunningham, Zarazuela , Lecoquierre, François , Schmid, Jana Pachlopnik , Kuhns, Douglas B. , Xu, Xuehua , Al–Herz, Waleed , Terhal, Paulien A., Muurinen, Mari , Barlogis, Vincent , Danielson, Jeffrey J. , Stewart, Helen , Rading, Sebastian, Keren, Boris , Pfundt, Rolph , Potocki, Lorraine , Olivier, Kenneth N., Faivre, Laurence , Wong, Melanie , Puel, Anne , Chou, Janet , Tusseau, Maud, Moutsopoulos, Niki M. , Matthews, Helen, Simons, Cas , Fink, Danielle , Kong, Heidi H. , Kabát, Juraj , Kim, Woo Sung , Bierhals, Tatjana , Meguro, Kazuyuki , Gu, Jingwen , Stoddard, Jennifer , Banos-Pinero, Benito, Slack, Maria A., Trivellin, Giampaolo , Mazel, Benoît , Li, Samuel T. , Watts, Val J. , Rodriguez-Quevedo, Maria F. , Bruel, Ange‐Line , Lehalle, Daphné , Torres, Daniel , Sullivan, Kathleen E. , Duffourd, Yannis, Similuk, Morgan , Blanc, Pierre , Jin, Tian, Geha, Raif S., Casanova, Jean‐Laurent , Mäkitie, Outi , Edery, Patrick , Germain, Ronald N. , Billadeau, Daniel D. , Zhang, Yu , Lenardo, Michael J. , Kober, Megan M , Koval, Alexey , Anderson, D Eric , Druey, Kirk M , Mandl, Judith N , Isidor, Bertrand , Ferreira, Carlos R , Freeman, Alexandra F , Karsak, Meliha , Mustillo, Peter J , Teo, Juliana , Chatron, Nicolas , Lecoquierre, Francois , Oler, Andrew J , Schmid, Jana Pachlopnik , Kuhns, Douglas B , Xu, Xuehua , Hauck, Fabian , Al-Herz, Waleed , Wagner, Matias , Terhal, Paulien A , Muurinen, Mari , Barlogis, Vincent , Loid, Petra , Keren, Boris , Pfundt, Rolph , Zarember, Kol A , Vill, Katharina , Olivier, Kenneth N , Lesca, Gaetan , Faivre, Laurence , Puel, Anne , Chou, Janet , Moutsopoulos, Niki M , Simons, Cas , Soldatos, Ariane , Masle-Farquhar, Etienne , Pittaluga, Stefania , Brink, Robert , Kong, Heidi H , Kabat, Juraj , Bierhals, Tatjana , Hsu, Amy P. , Gu, Jingwen , Trivellin, Giampaolo , Mazel, Benoît , Soomann, Maarja , Li, Samuel , Watts, Val J , Stratakis, Constantine A , Rodriguez-Quevedo, Maria F , Bruel, Ange-Line , Lipsanen-Nyman, Marita , Saultier, Paul , Lehalle, Daphne , Torres, Daniel , Barbarot, Sébastien , Neu, Axel , Similuk, Morgan N , McWalter, Kirsty , Blanc, Pierre , Bézieau, Stéphane , Geha, Raif S , Casanova, Jean Laurent , Makitie, Outi M , Edery, Patrick , Christodoulou, John , Germain, Ronald N , Goodnow, Christopher C , Sakmar, Thomas P , Billadeau, Daniel D , Kury, Sebastien , Katanaev, Vladimir L , Zhang, Yu , Lenardo, Michael J , Su, Helen C , Berchiche, Yamina A. , Wagner, Matias , Cruz, Phillip , Lesca, Gaëtan , Tusseau, Maud , Taft, Ryan J. , Pittaluga, Stefania , Baños-Piñero, Benito, Stratakis, Constantine A. , Jain, Rashmi, Bezieau, Stéphane , Jin, Tian , Kubisch, Christian , Küry, Sébastien , Su, Helen C.

Science | September 19, 2024 | Volume: 385 | Issue: 6715 | Pages: No page available

10.1126/science.add8947 Get It

Humans with monogenic inborn errors responsible for extreme disease phenotypes can reveal essential physiological pathways. We investigated germline mutations in GNAI2 , which encodes G αi2 , a key component in heterotrimeric G protein signal transduction usually thought to regulate adenylyl cyclase–mediated cyclic adenosine monophosphate (cAMP) production. Patients with activating G αi2 mutations had clinical presentations that included impaired immunity. Mutant G αi2 impaired cell migration and augmented responses to T cell receptor (TCR) stimulation. We found that mutant G αi2 influenced TCR signaling by sequestering the guanosine triphosphatase (GTPase)–activating protein RASA2, thereby promoting RAS activation and increasing downstream extracellular signal–regulated kinase (ERK)/mitogen-activated protein kinase (MAPK) and phosphatidylinositol 3-kinase (PI3K)–AKT S6 signaling to drive cellular growth and proliferation.
Variants in CLDN5 cause a syndrome characterized by seizures, microcephaly and brain calcifications
Deshwar, Ashish R. , Cytrynbaum, Cheryl , Murthy, Harsha, Zon, Jessica, Volpatti, Jonathan, Newbury‐Ecob, Ruth , Yu, Emily, Walker, Suzi, Scherer, Stephen W. , Mahida, Sonal , Elitt, Christopher M. , Nicolas, Gaël , Goldenberg, Alice , Saugier-Véber, Pascale , Lecoquierre, François , Dabaj, Ivana , Meddaugh, Hannah, Marble, Michael , Keppler‐Noreuil, Kim M. , Drayson, Lucy, Barañano, Kristin , Chassevent, Anna , Agre, Katie, Létard, Pascaline , Laquerrière, Annie, Ramsey, Keri , Henderson, Lindsay B. , Brady, Lauren , Tarnopolsky, Mark A. , Bainbridge, Matthew N. , Friedman, Jennifer , Capri, Yline , Athayde, Larissa Sampaio de, Ramos, Luiza , Blaser, Susan , Scherer, Stephen W , Nicolas, Gaël , Dabaj, Ivana , Dowling, James J , Lecoquierre, Francois , Tarnopolsky, Mark , Chitayat, David A. , Ellard, Sian , Allen, Hana Lango , Noche, Ramil R. , Bilan, Frédéric , Guyader, Gwenaël Le , Kok, Fernando , Gurgel‐Giannetti, Juliana , Weksberg, Rosanna

Brain | December 8, 2022 | Volume: 146 | Issue: 6 | Pages: 2285-2297

10.1093/brain/awac461 Get It

Abstract The blood–brain barrier ensures CNS homeostasis and protection from injury. Claudin-5 (CLDN5), an important component of tight junctions, is critical for the integrity of the blood–brain barrier. We have identified de novo heterozygous missense variants in CLDN5 in 15 unrelated patients who presented with a shared constellation of features including developmental delay, seizures (primarily infantile onset focal epilepsy), microcephaly and a recognizable pattern of pontine atrophy and brain calcifications. All variants clustered in one subregion/domain of the CLDN5 gene and the recurrent variants demonstrate genotype–phenotype correlations. We modelled both patient variants and loss of function alleles in the zebrafish to show that the variants analogous to those in patients probably result in a novel aberrant function in CLDN5. In total, human patient and zebrafish data provide parallel evidence that pathogenic sequence variants in CLDN5 cause a novel neurodevelopmental disorder involving disruption of the blood–brain barrier and impaired neuronal function.
Heterozygous variants in PRPF8 are associated with neurodevelopmental disorders
O’Grady, Lauren , Vergano, Samantha A. Schrier , Hoffman, Trevor L. , Sarco, Dean, Cherny, Sara , Bryant, Emily , Schultz‐Rogers, Laura , Sacharow, Stephanie , Immken, LaDonna, Holder, Susan, Blackwell, Rebecca R., Buchanan, Catherine A., Yusupov, Roman, Lecoquierre, François , Guerrot, Anne‐Marie , Rodan, Lance H. , Vries, Bert B.A. de , Kamsteeg, Erik Jan, Palomares‐Bralo, María , Brown, Natasha J. , Klee, Eric W. , Babovic‐Vuksanovic, Dusica , Rhodes, Lindsay, Person, Richard, Begtrup, Amber, Keller‐Ramey, Jennifer, Santiago‐Sim, Teresa, Schnur, Rhonda E. , Gold, Nina B. , Schrier Vergano, Samantha , Lecoquierre, Francois , Rodan, Lance , de Vries, Bert B A , Santos Simarro, Fernando , Palomares-Bralo, Maria , Babovic-Vuksanovic, Dusica, Sweetser, David A , Chung, Wendy K. , Pais, Lynn , Ferrer, Alejandro , Begtrup, Amber Hogart

American Journal of Medical Genetics Part A | May 11, 2022 | Volume: 188 | Issue: 9 | Pages: 2750-2759

10.1002/ajmg.a.62772 Get It

Abstract The pre‐mRNA‐processing factor 8, encoded by PRPF8, is a scaffolding component of a spliceosome complex involved in the removal of introns from mRNA precursors. Previously, heterozygous pathogenic variants in PRPF8 have been associated with autosomal dominant retinitis pigmentosa. More recently, PRPF8 was suggested as a candidate gene for autism spectrum disorder due to the enrichment of sequence variants in this gene in individuals with neurodevelopmental disorders. We report 14 individuals with various forms of neurodevelopmental conditions, found to have heterozygous, predominantly de novo, missense, and loss‐of‐function variants in PRPF8 . These individuals have clinical features that may represent a new neurodevelopmental syndrome.
De novo coding variants in the AGO1 gene cause a neurodevelopmental disorder with intellectual disability
Schalk, Audrey , Cousin, Margot A. , Dsouza, Nikita R., Challman, Thomas D. , Wain, Karen E. , Powis, Zöe , Minks, Kelly Q., Trimouille, Aurélien , Lasseaux, Eulalie , Michaud, Vincent , Van‐Gils, Julien , Spataro, Nino , Gabau, Elizabeth, Stolerman, Elliot , Washington, Camerun , Louie, Ray, Lanpher, Brendan C. , Kemppainen, Jennifer L., Innes, Micheil, Kooy, R. Frank , Goldenberg, Alice, Lecoquierre, François , Vera, Gabriella , Sheidley, Beth Rosen , Achkar, Christelle Moufawad El , Park, Meredith, Hamdan, Fadi F. , Michaud, Jacques L. , Lewis, Ann J., Zweier, Christiane , Wagner, Matias , Weigand, Heike, Journel, Hubert, Keren, Boris , Passemard, Sandrine , Mignot, Cyril , Brilstra, Eva H. , Itzikowitz, Gina, O’Heir, Emily , Allen, Jake, Donald, Kirsten A. , Korf, Bruce R. , Skelton, Tammi, Rudy, Natasha L. , Dobyns, William B. , Foss, Kimberly , Bosanko, Katherine A. , Alembik, Yves, Durand, Benjamin , Mau‐Them, Frédéric Tran , Ranza, Emmanuelle , Blanc, Xavier , Torti, Erin , Millan, Francisca , Dameron, Amy, Tokita, Mari, Zimmermann, Michael T. , Klee, Eric W. , Piton, Amélie , Gérard, Bénédicte , Ruiz, Anna , Stolerman, Elliot , Kooy, Frank , Lecoquierre, Francois , Reis, André , Wagner, Matias , Passemard, Sandrine , Tran Mau-Them, Frederic , Klee, Eric W , Piton, Amelie , Zimmermann, Michael T , Lacombe, Didier , Angelini, Chloé , Louie, Raymond J. , Meuwissen, Marije E. C. , Goldenberg, Alice , Diderich, Karin E. M. , Reis, André , Gassen, Koen L.I. van , Thompson, Michelle L. , Robin, Nathaniel H. , Zárate, Yuri A. , Antonarakis, Stylianos E. , McWalter, Kirsty

Journal of Medical Genetics | December 20, 2021 | Volume: 59 | Issue: 10 | Pages: 965-975

10.1136/jmedgenet-2021-107751 Get It

Background High-impact pathogenic variants in more than a thousand genes are involved in Mendelian forms of neurodevelopmental disorders (NDD). Methods This study describes the molecular and clinical characterisation of 28 probands with NDD harbouring heterozygous AGO1 coding variants, occurring de novo for all those whose transmission could have been verified (26/28). Results A total of 15 unique variants leading to amino acid changes or deletions were identified: 12 missense variants, two in-frame deletions of one codon, and one canonical splice variant leading to a deletion of two amino acid residues. Recurrently identified variants were present in several unrelated individuals: p.(Phe180del), p.(Leu190Pro), p.(Leu190Arg), p.(Gly199Ser), p.(Val254Ile) and p.(Glu376del). AGO1 encodes the Argonaute 1 protein, which functions in gene-silencing pathways mediated by small non-coding RNAs. Three-dimensional protein structure predictions suggest that these variants might alter the flexibility of the AGO1 linker domains, which likely would impair its function in mRNA processing. Affected individuals present with intellectual disability of varying severity, as well as speech and motor delay, autistic behaviour and additional behavioural manifestations. Conclusion Our study establishes that de novo coding variants in AGO1 are involved in a novel monogenic form of NDD, highly similar to the recently reported AGO2 -related NDD.
NGLY1 Deficiency: A Rare Newly Described Condition with a Typical Presentation
Dabaj, Ivana , Sudrié‐Arnaud, Bénédicte , Lecoquierre, François , Raymond, Kimiyo , Ducatez, Franklin , Guerrot, Anne‐Marie , Snanoudj, Sarah , Coutant, Sophie , Saugier-Véber, Pascale , Marret, Stéphane , Tebani, Abdellah , Bekri, Soumeya , Bekri, Soumeya , Lecoquierre, Francois , Dabaj, Ivana , Nicolas, Gaël

Life | February 27, 2021 | Volume: 11 | Issue: 3 | Pages: 187

10.3390/life11030187 Get It

NGLY1 deficiency is the first recognized autosomal recessive disorder of N-linked deglycosylation (NGLY1-CDDG). This severe multisystemic disease is still poorly known and, to date, most cases have been diagnosed through whole exome or genome sequencing. The aim of this study is to provide the clinical, biochemical and molecular description of the first NGLY1-CDDG patient from France along with a literature review. The index case presented with developmental delay, acquired microcephaly, hypotonia, alacrimia, feeding difficulty, and dysmorphic features. Given the complex clinical picture and the multisystemic involvement, a trio-based exome sequencing was conducted and urine oligosaccharides were assessed using mass spectrometry. The exome sequencing revealed a novel variant in the NGLY1 gene in a homozygous state. NGLY1 deficiency was confirmed by the identification of the Neu5Ac1Hex1GlcNAc1-Asn oligosaccharide in the urine of the patient. Literature review revealed the association of some key clinical and biological features such as global developmental delay—hypertransaminasemia, movement disorders, feeding difficulties and alacrima/hypolacrima.