Pathological phosphorylation of tau and TDP-43 by TTBK1 and TTBK2 drives neurodegeneration
Tóm tắt
Từ khóa
Tài liệu tham khảo
Burrell JR, Kiernan MC, Vucic S, Hodges JR. Motor neuron dysfunction in frontotemporal dementia. Brain. 2011;134:2582–94.
Sieben A, Van Langenhove T, Engelborghs S, Martin JJ, Boon P, Cras P, et al. The genetics and neuropathology of frontotemporal lobar degeneration. Acta Neuropathol. 2012;124:353–72.
Hong M, Zhukareva V, Vogelsberg-Ragaglia V, Wszolek Z, Reed L, Miller BI, et al. Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17. Science. 1998;282:1914–7.
Neumann M, Kwong LK, Lee EB, Kremmer E, Flatley A, Xu Y, et al. Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies. Acta Neuropathol. 2009;117:137–49.
Ayala YM, Zago P, D'Ambrogio A, Xu YF, Petrucelli L, Buratti E, et al. Structural determinants of the cellular localization and shuttling of TDP-43. J Cell Sci. 2008;121:3778–85.
Brady OA, Meng P, Zheng Y, Mao Y, Hu F. Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1. J Neurochem. 2011;116:248–59.
Hasegawa M, Arai T, Nonaka T, Kametani F, Yoshida M, Hashizume Y, et al. Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann Neurol. 2008;64:60–70.
Liachko NF, Guthrie CR, Kraemer BC. Phosphorylation promotes neurotoxicity in a Caenorhabditis Elegans model of TDP-43 Proteinopathy. J Neurosci. 2010;30:16208–19.
Liachko NF, PJ MM, Strovas TJ, Loomis E, Greenup L, Murrell JR, et al. The tau tubulin kinases TTBK1/2 promote accumulation of pathological TDP-43. PLoS Genet. 2014;10:e1004803.
Alonso AC, Grundke-Iqbal I, Iqbal K. Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat Med. 1996;2:783–7.
Chatterjee S, Sang TK, Lawless GM, Jackson GR. Dissociation of tau toxicity and phosphorylation: role of GSK-3beta, MARK and Cdk5 in a drosophila model. Hum Mol Genet. 2009;18:164–77.
Grundke-Iqbal I, Iqbal K, Tung YC, Quinlan M, Wisniewski HM, Binder LI. Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc Natl Acad Sci U S A. 1986;83:4913–7.
Köpke E, Tung YC, Shaikh S, Alonso AC, Iqbal K, Grundke-Iqbal I. Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J Biol Chem. 1993;268:24374–84.
Kraemer BC, Zhang B, Leverenz JB, Thomas JH, Trojanowski JQ, Schellenberg GD. Neurodegeneration and defective neurotransmission in a Caenorhabditis Elegans model of tauopathy. Proc Natl Acad Sci U S A. 2003;100:9980–5.
Vega IE, Cui L, Propst JA, Hutton ML, Lee G, Yen SH. Increase in tau tyrosine phosphorylation correlates with the formation of tau aggregates. Brain Res Mol Brain Res. 2005;138:135–44.
Lund H, Cowburn RF, Gustafsson E, Stromberg K, Svensson A, Dahllund L, et al. Tau-tubulin kinase 1 expression, phosphorylation and co-localization with phospho-Ser422 tau in the Alzheimer's disease brain. Brain Pathol. 2013;23:378–89.
Sato S, Cerny RL, Buescher JL, Ikezu T. Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is involved in tau phosphorylation and aggregation. J Neurochem. 2006;98:1573–84.
Sato S, Xu J, Okuyama S, Martinez LB, Walsh SM, Jacobsen MT, et al. Spatial learning impairment, enhanced CDK5/p35 activity, and downregulation of NMDA receptor expression in transgenic mice expressing tau-tubulin kinase 1. J Neurosci. 2008;28:14511–21.
Asai H, Ikezu S, Woodbury ME, Yonemoto GM, Cui L, Ikezu T. Accelerated neurodegeneration and neuroinflammation in transgenic mice expressing P301L tau mutant and tau-tubulin kinase 1. Am J Pathol. 2014;184:808–18.
Houlden H, Johnson J, Gardner-Thorpe C, Lashley T, Hernandez D, Worth P, et al. Mutations in TTBK2, encoding a kinase implicated in tau phosphorylation, segregate with spinocerebellar ataxia type 11. Nat Genet. 2007;39:1434–6.
Čajánek L, Nigg EA. Cep164 triggers ciliogenesis by recruiting tau tubulin kinase 2 to the mother centriole. Proc Natl Acad Sci U S A. 2014;111:E2841–50.
Oda T, Chiba S, Nagai T, Mizuno K. Binding to Cep164, but not EB1, is essential for centriolar localization of TTBK2 and its function in ciliogenesis. Genes Cells. 2014;19:927–40.
Watanabe T, Kakeno M, Matsui T, Sugiyama I, Arimura N, Matsuzawa K, et al. TTBK2 with EB1/3 regulates microtubule dynamics in migrating cells through KIF2A phosphorylation. J Cell Biol. 2015;210:737–51.
Tomizawa K, Omori A, Ohtake A, Sato K, Takahashi M. Tau-tubulin kinase phosphorylates tau at Ser-208 and Ser-210, sites found in paired helical filament-tau. FEBS Lett. 2001;492:221–7.
Cinar H, Keles S, Jin Y. Expression profiling of GABAergic motor neurons in Caenorhabditis Elegans. Curr Biol. 2005;15:340–6.
Ishihara T, Hong M, Zhang B, Nakagawa Y, Lee MK, Trojanowski JQ, et al. Age-dependent emergence and progression of a tauopathy in transgenic mice overexpressing the shortest human tau isoform. Neuron. 1999;24:751–62.
Greenberg SG, Davies P. A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis. Proc Natl Acad Sci U S A. 1990;87:5827–31.
Liachko NF, PJ MM, Guthrie CR, Bird TD, Leverenz JB, Kraemer BC. CDC7 inhibition blocks pathological TDP-43 phosphorylation and neurodegeneration. Ann Neurol. 2013;74:39–52.
Cohen P. Protein kinases--the major drug targets of the twenty-first century? Nat Rev Drug Discov. 2002;1:309–15.
Tsai LH, Takahashi T, Caviness VS, Harlow E. Activity and expression pattern of cyclin-dependent kinase 5 in the embryonic mouse nervous system. Development. 1993;119:1029–40.