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Glycogen synthase kinase 3 phosphorylation of different residues in the presence of different factors: analysis on tau protein.

Abstract：

:Several peptides derived from microtubule-associated tau protein, have been tested as substrates for glycogen synthase kinase 3 (GSK 3). In the absence of cofactors, GSK 3 can modify serines or threonines followed by prolines. In other cases, a phosphorylation in position +4 is required for the phosphorylation of threonine/serine residues. A third type of substrate can be modified by GSK 3 in the presence of heparin. The comparison of GSK 3 with other kinases suggests some similar features of this kinase with proline-directed protein kinases, such as cdc-2 or mitogen-activated protein kinase (MAP Kinases,) and also with casein kinase 2 (CK 2). Thus, all these kinases are specifically inhibited by 5,6-Dichloro-1-(beta-D-ribofuranosyl)-benzimidazole (DRB). However, heparin is an inhibitor of CK 2 whereas it activates the modification of certain substrates by GSK 3. A possible explanation for the obtained results is that the consensus sequence for GSK 3 phosphorylation is a serine/threonine adjacent to a proline or other beta-turn former residue and that such recognition could be favoured by the presence of adjacent negative charges or the addition of polyanions.

journal_name

Mol Cell Biochem

journal_title

Molecular and cellular biochemistry

authors

Moreno FJ,Muñoz-Montaño JR,Avila J

doi

10.1007/BF00229744

subject

Has Abstract

pub_date

1996-12-06 00:00:00

pages

47-54

issue

1

eissn

0300-8177

issn

1573-4919

journal_volume

165

pub_type

杂志文章

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