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Site Information |
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kVtskCGsLGNIHHk SwissProt Entrez-Gene |
Blast this site against: NCBI SwissProt PDB |
Site Group ID: 449328 |
In vivo Characterization | |
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Methods used to characterize site in vivo: | |
Disease tissue studied: | |
Relevant cell line - cell type - tissue: |
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Downstream Regulation | |
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Effects of modification on Tau iso8: | |
Effects of modification on biological processes: |
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Relevant diseases: |
References | |
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Kao DS, et al. (2022) Identification of novel kinases of Tau using fluorescence complementation mass spectrometry (FCMS). Mol Cell Proteomics 21, 100441
36379402 Curated Info |
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Hochmair J, et al. (2022) Molecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates. EMBO J, e108882
35298090 Curated Info |
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Carlomagno Y, et al. (2017) An acetylation-phosphorylation switch that regulates tau aggregation propensity and function. J Biol Chem 292, 15277-15286
28760828 Curated Info |
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Tugaeva KV, Tsvetkov PO, Sluchanko NN (2017) Bacterial co-expression of human Tau protein with protein kinase A and 14-3-3 for studies of 14-3-3/phospho-Tau interaction. PLoS One 12, e0178933
28575131 Curated Info |
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Thornton C, et al. (2011) AMP-activated protein kinase (AMPK) is a tau kinase, activated in response to amyloid β-peptide exposure. Biochem J 434, 503-12
21204788 Curated Info |
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Hanger DP, et al. (2007) Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis. J Biol Chem 282, 23645-54
17562708 Curated Info |
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Taniguchi T, et al. (2001) Phosphorylation of tau is regulated by PKN. J Biol Chem 276, 10025-31
11104762 Curated Info |
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Schneider A, et al. (1999) Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. Biochemistry 38, 3549-58
10090741 Curated Info |
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Illenberger S, et al. (1998) The endogenous and cell cycle-dependent phosphorylation of tau protein in living cells: implications for Alzheimer's disease. Mol Biol Cell 9, 1495-512
9614189 Curated Info |
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Drewes G, et al. (1997) MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell 89, 297-308
9108484 Curated Info |
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Drewes G, et al. (1995) Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. J Biol Chem 270, 7679-88
7706316 Curated Info |
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Abreha MH, et al. TBK1 interacts with tau and enhances neurodegeneration in tauopathy. J Biol Chem 296, 100760
33965374 Curated Info |