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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1994-3-11
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pubmed:abstractText |
The alpha-isoform of glycogen synthase kinase-3 (GSK3 alpha) was inactivated by 80% towards a synthetic peptide substrate upon incubation with Mg-ATP and either MAP kinase-activated protein (MAPKAP) kinase-1 or p70 S6 kinase. Inactivation by either kinase resulted from the phosphorylation of Ser-21 and was reversed by treatment with protein phosphatase 2A1. Phosphorylation also decreased GSK3 alpha activity towards glycogen synthase, inhibitor-2 and c-jun. The specificity of GSK3 alpha was similar to GSK3 beta, but with the synthetic peptide substrate heparin stimulated the dephosphorylated form of GSK3 alpha (6-fold) more than GSK3 beta (1.8-fold). After phosphorylation, both isoforms were stimulated 15-20-fold by heparin.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
338
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
37-42
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8307153-Amino Acid Sequence,
pubmed-meshheading:8307153-Animals,
pubmed-meshheading:8307153-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:8307153-Glycogen Synthase Kinase 3,
pubmed-meshheading:8307153-Glycogen Synthase Kinases,
pubmed-meshheading:8307153-Microtubule-Associated Proteins,
pubmed-meshheading:8307153-Molecular Sequence Data,
pubmed-meshheading:8307153-Muscles,
pubmed-meshheading:8307153-Phosphorylation,
pubmed-meshheading:8307153-Protein-Serine-Threonine Kinases,
pubmed-meshheading:8307153-Rabbits,
pubmed-meshheading:8307153-Ribosomal Protein S6 Kinases,
pubmed-meshheading:8307153-Ribosomal Protein S6 Kinases, 90-kDa
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pubmed:year |
1994
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pubmed:articleTitle |
The alpha-isoform of glycogen synthase kinase-3 from rabbit skeletal muscle is inactivated by p70 S6 kinase or MAP kinase-activated protein kinase-1 in vitro.
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pubmed:affiliation |
Department of Biochemistry, University of Dundee, Scotland, UK.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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