Sites of phosphorylation in tau and factors affecting their regulation
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 i...
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Published in | Biochemical Society Symposia no. 67; p. 73 |
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Main Authors | , , , , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
01.01.2001
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Abstract | 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. |
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AbstractList | 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. |
Author | Hanger, D P Chapman, S Brion, J P Anderton, B H Gibb, G Betts, J Reynolds, C H Van Slegtenhorst, M Connell, J Lovestone, S Mack, T Kardalinou, E Hutton, M Blackstock, W P Dayanandan, R Gallo, J M Leroy, K |
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SubjectTerms | Alzheimer Disease - metabolism Amino Acid Sequence Animals Binding Sites Calcium-Calmodulin-Dependent Protein Kinases - metabolism Cell Line COS Cells Glycogen Synthase Kinase 3 Glycogen Synthase Kinases Humans In Vitro Techniques Mitogen-Activated Protein Kinase 1 - metabolism Mitogen-Activated Protein Kinase 10 Mitogen-Activated Protein Kinases - metabolism Molecular Sequence Data Mutation Neurons - metabolism p38 Mitogen-Activated Protein Kinases Phosphorylation Protein-Tyrosine Kinases - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism tau Proteins - chemistry tau Proteins - genetics tau Proteins - metabolism Transfection |
Title | Sites of phosphorylation in tau and factors affecting their regulation |
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