Sites of phosphorylation in tau and factors affecting their regulation

C ONeill; B Anderton; W P Blackstock; J P Brion; S Chapman; J Connell; R Dayanandan; J M Gallo; G Gibb; D P Hanger; M Hutton; E Kardalinou; K Leroy; S Lovestone; T Mack; C H Reynolds; M Van Slegtenhorst

Sites of phosphorylation in tau and factors affecting their regulation

C ONeill, B Anderton (Editor), W P Blackstock, J P Brion, S Chapman, J Connell, R Dayanandan, J M Gallo, G Gibb, D P Hanger, M Hutton, E Kardalinou, K Leroy, S Lovestone, T Mack, C H Reynolds, M Van Slegtenhorst

Research output: Chapter in Book/Report/Conference proceeding › Conference paper

99 Citations (Scopus)

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 Arg(406)--> Trp (R406W) tau mutation also affects tau phosphorylation in cells.

Original language	English
Title of host publication	BIOCHEM SOC SYMPOSIUM
Place of Publication	LONDON
Publisher	PORTLAND PRESS LTD
Pages	73 - 80
Number of pages	8
ISBN (Print)	1-85578-133-6
Publication status	Published - 2001
Event	Annual Symposium of the Biochemical-Society - CORK, Ireland Duration: 1 Jan 2001 → …

Publication series

Name	BIOCHEMICAL SOCIETY SYMPOSIUM

Conference

Conference	Annual Symposium of the Biochemical-Society
Country/Territory	Ireland
City	CORK
Period	1/01/2001 → …

Cite this

ONeill, C., Anderton, B. (Ed.), Blackstock, W. P., Brion, J. P., Chapman, S., Connell, J., Dayanandan, R., Gallo, J. M., Gibb, G., Hanger, D. P., Hutton, M., Kardalinou, E., Leroy, K., Lovestone, S., Mack, T., Reynolds, C. H., & Van Slegtenhorst, M. (2001). Sites of phosphorylation in tau and factors affecting their regulation. In BIOCHEM SOC SYMPOSIUM (pp. 73 - 80). (BIOCHEMICAL SOCIETY SYMPOSIUM). PORTLAND PRESS LTD.

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title = "Sites of phosphorylation in tau and factors affecting their regulation",

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 Arg(406)--> Trp (R406W) tau mutation also affects tau phosphorylation in cells.",

author = "C ONeill and B Anderton and Blackstock, {W P} and Brion, {J P} and S Chapman and J Connell and R Dayanandan and Gallo, {J M} and G Gibb and Hanger, {D P} and M Hutton and E Kardalinou and K Leroy and S Lovestone and T Mack and Reynolds, {C H} and {Van Slegtenhorst}, M",

year = "2001",

language = "English",

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series = "BIOCHEMICAL SOCIETY SYMPOSIUM",

publisher = "PORTLAND PRESS LTD",

pages = "73 -- 80",

booktitle = "BIOCHEM SOC SYMPOSIUM",

note = "Annual Symposium of the Biochemical-Society ; Conference date: 01-01-2001",

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ONeill, C , Anderton, B (ed.), Blackstock, WP, Brion, JP, Chapman, S, Connell, J, Dayanandan, R, Gallo, JM, Gibb, G, Hanger, DP, Hutton, M, Kardalinou, E, Leroy, K, Lovestone, S, Mack, T, Reynolds, CH & Van Slegtenhorst, M 2001, Sites of phosphorylation in tau and factors affecting their regulation. in BIOCHEM SOC SYMPOSIUM. BIOCHEMICAL SOCIETY SYMPOSIUM, PORTLAND PRESS LTD, LONDON, pp. 73 - 80, Annual Symposium of the Biochemical-Society, CORK, Ireland, 1/01/2001.

TY - CHAP

T1 - Sites of phosphorylation in tau and factors affecting their regulation

AU - ONeill, C

AU - Blackstock, W P

AU - Brion, J P

AU - Chapman, S

AU - Connell, J

AU - Dayanandan, R

AU - Gallo, J M

AU - Gibb, G

AU - Hanger, D P

AU - Hutton, M

AU - Kardalinou, E

AU - Leroy, K

AU - Lovestone, S

AU - Mack, T

AU - Reynolds, C H

AU - Van Slegtenhorst, M

A2 - Anderton, B

PY - 2001

Y1 - 2001

N2 - 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 Arg(406)--> Trp (R406W) tau mutation also affects tau phosphorylation in cells.

AB - 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 Arg(406)--> Trp (R406W) tau mutation also affects tau phosphorylation in cells.

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M3 - Conference paper

SN - 1-85578-133-6

T3 - BIOCHEMICAL SOCIETY SYMPOSIUM

SP - 73

EP - 80

BT - BIOCHEM SOC SYMPOSIUM

PB - PORTLAND PRESS LTD

CY - LONDON

T2 - Annual Symposium of the Biochemical-Society

Y2 - 1 January 2001

ER -

Sites of phosphorylation in tau and factors affecting their regulation

Abstract

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Conference

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