Citations 2
Current directions in tau research: Highlights from Tau 2020
Sexton, Claire E. , Snyder, Heather M. , Boxer, Adam L. , Brannelly, Patrick , Brion, Jean‐Pierre , Buée, Luc , Cacace, Angela , Chételat, Gaël , Citron, Martin , DeVos, Sarah L. , Diaz, Kristophe , Feldman, Howard , Frost, Bess , Goate, Alison , Gold, Michael , Johnson, Keith A. , Kerwin, Diana , Mummery, Catherine J. , Mutamba, James, Quiroz, Yakeel T. , Rabinovici, Gil D. , Rommel, Amy, Shulman, Melanie , Toledo‐Sherman, Leticia , Weninger, Stacie, Wildsmith, Kristin R., Worley, Susan, Carrillo, María C. , Sexton, Claire , Patterson, Marc C. , Rabinovici, Gil D , Feldman, Howard H , Goate, Alison M , Beher, Dirk , Hyman, Bradley T. , Karch, Celeste M. , Koroshetz, Walter J. , Litvan, Irene , Morris, Huw R.
Alzheimer's & Dementia | September 28, 2021 | Volume: 18 | Issue: 5 | Pages: 988-1007
AbstractStudies supporting a strong association between tau deposition and neuronal loss, neurodegeneration, and cognitive decline have heightened the allure of tau and tau‐related mechanisms as therapeutic targets. In February 2020, leading tau experts from around the world convened for the first‐ever Tau2020 Global Conference in Washington, DC, co‐organized and cosponsored by the Rainwater Charitable Foundation, the Alzheimer's Association, and CurePSP. Representing academia, industry, government, and the philanthropic sector, presenters and attendees discussed recent advances and current directions in tau research. The meeting provided a unique opportunity to move tau research forward by fostering global partnerships among academia, industry, and other stakeholders and by providing support for new drug discovery programs, groundbreaking research, and emerging tau researchers. The meeting also provided an opportunity for experts to present critical research‐advancing tools and insights that are now rapidly accelerating the pace of tau research.
Sites of phosphorylation in tau and factors affecting their regulation
Anderton, Brian H., Blackstock, Walter, Chapman, Sara, Connell, James W., Dayanandan, Rejith, Gibb, Graham, Hutton, Mike, Kardalinou, Efterpi, Leroy, Karell, Mack, Till G.A., Reynolds, C. Hugh, Slegtenhorst, Marjon van, Betts, Joanna C. , Brion, Jean‐Pierre , Chapman, Sara, Gallo, Jean‐Marc , Hanger, Diane P. , Leroy, Karelle , Lovestone, Simon
Biochemical Society Symposia | August 10, 2015 | Volume: 67 | Issue: No issue available | Pages: 73-80
The microtubule-associated protein, tau, is the principal component of paired helical filaments (PHFs) in Alzheimer's disease. PHF-tau is highly phosphorylated and a total of 25 sites of phosphorylation have so far been identified. Many of these sites are serine or threonine residues that are immediately followed in the sequence by proline residues, and hence are candidate phosphorylation sites for proline-directed kinases. In vitro, glycogen synthase kinase-3 (GSK-3), extracellular signal-related kinase-1 and -2, and mitogen-activated protein kinases, p38 kinase and c-jun N-terminal kinase, all phosphorylate many of these sites, although with different efficiencies for particular sites. Phosphorylation studies in transfected cells and neurons show that GSK-3 phosphorylates tau more extensively than do these other proline-directed kinases. Mutations in tau have been shown to affect in vitro phosphorylation of tau by GSK-3. The Arg406-->Trp (R406W) tau mutation also affects tau phosphorylation in cells.