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Phosphorylation of tau by cyclic-AMP-dependent protein kinase

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Phosphorylation of tau by cyclic-AMP-dependent protein kinase. / Robertson, J.; Loviny, T. L F; Goedert, M.; Jakes, R.; Murray, K. J.; Anderton, B. H.; Hanger, D. P.

In: Dementia, Vol. 4, No. 5, 01.01.1993, p. 256-263.

Research output: Contribution to journalArticle

Harvard

Robertson, J, Loviny, TLF, Goedert, M, Jakes, R, Murray, KJ, Anderton, BH & Hanger, DP 1993, 'Phosphorylation of tau by cyclic-AMP-dependent protein kinase', Dementia, vol. 4, no. 5, pp. 256-263.

APA

Robertson, J., Loviny, T. L. F., Goedert, M., Jakes, R., Murray, K. J., Anderton, B. H., & Hanger, D. P. (1993). Phosphorylation of tau by cyclic-AMP-dependent protein kinase. Dementia, 4(5), 256-263.

Vancouver

Robertson J, Loviny TLF, Goedert M, Jakes R, Murray KJ, Anderton BH et al. Phosphorylation of tau by cyclic-AMP-dependent protein kinase. Dementia. 1993 Jan 1;4(5):256-263.

Author

Robertson, J. ; Loviny, T. L F ; Goedert, M. ; Jakes, R. ; Murray, K. J. ; Anderton, B. H. ; Hanger, D. P. / Phosphorylation of tau by cyclic-AMP-dependent protein kinase. In: Dementia. 1993 ; Vol. 4, No. 5. pp. 256-263.

Bibtex Download

@article{064f8e495e1a42fdadd8c00deed7b017,
title = "Phosphorylation of tau by cyclic-AMP-dependent protein kinase",
abstract = "Alzheimer's disease paired helical filaments contain abnormally phosphorylated tau (PHF-tau) which has reduced electrophoretic mobility on sodium dodecyl sulphate polyacrylamide electrophoresis. We have investigated the effects of cyclic-AMP-dependent protein kinase (PKA) on recombinant human tau isoforms and two recombinant tau fragments. PKA phosphorylated tau and reduced its electrophoretic mobility, phosphorylation towards the C-terminus of tau having a major influence on this property. Substitution of serine396 (phosphorylated in PHF-tau) or serine416 (phosphorylated by calcium/calmodulin kinase II) by alanine demonstrated that these are not major sites for PKA phosphorylation. Although the phosphorylated forms of tau generated by PKA are not identical to those of PHF-tau, PKA may be involved in the generation of PHF-tau in Alzheimer's disease via phosphorylation of additional, as yet unidentified, sites on tau.",
keywords = "Alzheimer's disease, Cyclic-AMP-dependent protein kinase, Microtubule-associated proteins, Protein phosphorylation, Tau",
author = "J. Robertson and Loviny, {T. L F} and M. Goedert and R. Jakes and Murray, {K. J.} and Anderton, {B. H.} and Hanger, {D. P.}",
year = "1993",
month = jan,
day = "1",
language = "English",
volume = "4",
pages = "256--263",
journal = "Dementia",
issn = "1013-7424",
publisher = "S. Karger AG",
number = "5",

}

RIS (suitable for import to EndNote) Download

TY - JOUR

T1 - Phosphorylation of tau by cyclic-AMP-dependent protein kinase

AU - Robertson, J.

AU - Loviny, T. L F

AU - Goedert, M.

AU - Jakes, R.

AU - Murray, K. J.

AU - Anderton, B. H.

AU - Hanger, D. P.

PY - 1993/1/1

Y1 - 1993/1/1

N2 - Alzheimer's disease paired helical filaments contain abnormally phosphorylated tau (PHF-tau) which has reduced electrophoretic mobility on sodium dodecyl sulphate polyacrylamide electrophoresis. We have investigated the effects of cyclic-AMP-dependent protein kinase (PKA) on recombinant human tau isoforms and two recombinant tau fragments. PKA phosphorylated tau and reduced its electrophoretic mobility, phosphorylation towards the C-terminus of tau having a major influence on this property. Substitution of serine396 (phosphorylated in PHF-tau) or serine416 (phosphorylated by calcium/calmodulin kinase II) by alanine demonstrated that these are not major sites for PKA phosphorylation. Although the phosphorylated forms of tau generated by PKA are not identical to those of PHF-tau, PKA may be involved in the generation of PHF-tau in Alzheimer's disease via phosphorylation of additional, as yet unidentified, sites on tau.

AB - Alzheimer's disease paired helical filaments contain abnormally phosphorylated tau (PHF-tau) which has reduced electrophoretic mobility on sodium dodecyl sulphate polyacrylamide electrophoresis. We have investigated the effects of cyclic-AMP-dependent protein kinase (PKA) on recombinant human tau isoforms and two recombinant tau fragments. PKA phosphorylated tau and reduced its electrophoretic mobility, phosphorylation towards the C-terminus of tau having a major influence on this property. Substitution of serine396 (phosphorylated in PHF-tau) or serine416 (phosphorylated by calcium/calmodulin kinase II) by alanine demonstrated that these are not major sites for PKA phosphorylation. Although the phosphorylated forms of tau generated by PKA are not identical to those of PHF-tau, PKA may be involved in the generation of PHF-tau in Alzheimer's disease via phosphorylation of additional, as yet unidentified, sites on tau.

KW - Alzheimer's disease

KW - Cyclic-AMP-dependent protein kinase

KW - Microtubule-associated proteins

KW - Protein phosphorylation

KW - Tau

UR - http://www.scopus.com/inward/record.url?scp=0027268652&partnerID=8YFLogxK

M3 - Article

C2 - 8261023

AN - SCOPUS:0027268652

VL - 4

SP - 256

EP - 263

JO - Dementia

JF - Dementia

SN - 1013-7424

IS - 5

ER -

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