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Glycogen synthase kinase 3 phosphorylates recombinant human tau protein at serine‐262 in the presence of heparin (or tubulin)
Author(s) -
Moreno Francisco J.,
Medina Miguel,
Pérez Mar,
Montejo de Garcini Esteban,
Avila Jesús
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00934-2
Subject(s) - gsk 3 , tubulin , glycogen synthase , phosphorylation , biochemistry , serine , protein kinase a , kinase , gsk3b , chemistry , biology , microbiology and biotechnology , microtubule
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.