Glycogen synthase kinase 3 phosphorylates recombinant human tau protein at serine-262 in the presence of heparin (or tubulin)
- PMID: 7556645
- DOI: 10.1016/0014-5793(95)00934-2
Glycogen synthase kinase 3 phosphorylates recombinant human tau protein at serine-262 in the presence of heparin (or tubulin)
Abstract
Tau protein, the major component of the aberrant structures termed paired helical filaments (PHFs) present in the brain of Alzheimer's disease patients, is pathologically phosphorylated in sites in and around the tubulin-binding sites. A single protein kinase, glycogen synthase kinase 3 (GSK 3), is able to phosphorylate tau at the flanking regions and, additionally, at the tubulin-binding motifs if heparin or tubulin is present. Serines-262 and -324 have been found to be modified at the tubulin-binding region of tau protein by GSK 3 in the presence of heparin or tubulin.
Similar articles
-
Protein kinase FA/glycogen synthase kinase-3 alpha after heparin potentiation phosphorylates tau on sites abnormally phosphorylated in Alzheimer's disease brain.J Neurochem. 1994 Oct;63(4):1416-25. doi: 10.1046/j.1471-4159.1994.63041416.x. J Neurochem. 1994. PMID: 7931292
-
Phosphorylation of microtubule-associated protein tau by Ca2+/calmodulin-dependent protein kinase II in its tubulin binding sites.Arch Biochem Biophys. 2002 Dec 15;408(2):255-62. doi: 10.1016/s0003-9861(02)00556-8. Arch Biochem Biophys. 2002. PMID: 12464279
-
Tau protein kinase I/GSK-3 beta/kinase FA in heparin phosphorylates tau on Ser199, Thr231, Ser235, Ser262, Ser369, and Ser400 sites phosphorylated in Alzheimer disease brain.J Protein Chem. 1995 Feb;14(2):95-105. doi: 10.1007/BF01888367. J Protein Chem. 1995. PMID: 7786411
-
Microtubule-associated protein tau, paired helical filaments, and phosphorylation.Ann N Y Acad Sci. 1993 Sep 24;695:209-16. doi: 10.1111/j.1749-6632.1993.tb23054.x. Ann N Y Acad Sci. 1993. PMID: 7694533 Review.
-
Physiology and pathology of tau protein kinases in relation to Alzheimer's disease.J Biochem. 1997 Feb;121(2):179-88. J Biochem. 1997. PMID: 9089387 Review.
Cited by
-
Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration.Biochem J. 1997 May 1;323 ( Pt 3)(Pt 3):577-91. doi: 10.1042/bj3230577. Biochem J. 1997. PMID: 9169588 Free PMC article. Review.
-
Regulation of phosphorylation of tau by cyclin-dependent kinase 5 and glycogen synthase kinase-3 at substrate level.FEBS Lett. 2006 Oct 30;580(25):5925-33. doi: 10.1016/j.febslet.2006.09.060. Epub 2006 Oct 5. FEBS Lett. 2006. PMID: 17045592 Free PMC article.
-
Glycogen Synthase Kinase-3β, NLRP3 Inflammasome, and Alzheimer's Disease.Curr Med Sci. 2023 Oct;43(5):847-854. doi: 10.1007/s11596-023-2788-4. Epub 2023 Sep 18. Curr Med Sci. 2023. PMID: 37721665
-
Phosphorylation of tau by glycogen synthase kinase 3beta affects the ability of tau to promote microtubule self-assembly.Biochem J. 1997 May 1;323 ( Pt 3)(Pt 3):741-7. doi: 10.1042/bj3230741. Biochem J. 1997. PMID: 9169608 Free PMC article.
-
GSK-3 in Neurodegenerative Diseases.Int J Alzheimers Dis. 2011;2011:189246. doi: 10.4061/2011/189246. Epub 2011 May 4. Int J Alzheimers Dis. 2011. PMID: 21629738 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Medical