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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1997-12-8
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pubmed:abstractText |
293 cells were transfected with wild-type GSK3beta (WT-GSK3beta) or a mutant in which the PKB phosphorylation site (Ser-9) was altered to Ala (A9-GSK3beta). Upon stimulation with IGF-1 or insulin, WT-GSK3beta was inhibited 75% or 60%, respectively, whereas the activity of the A9-GSK3beta mutant was unaffected. Incubation of WT-GSK3beta with PP2A1 (a Ser/Thr-specific phosphatase) completely reversed the IGF-1- or insulin-induced inhibition. IGF-1 stimulation did not induce any tyrosine dephosphorylation of WT-GSK3beta or A9-GSK3beta. Coexpression of WT-GSK3beta in 293 cells with either PKB alpha (also known as AKT) or PDK1 (the 'upstream' activator of PKB) mimicked the IGF-1- or insulin-induced phosphorylation of Ser-9 and inactivation of GSK3beta.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/3-phosphoinositide-dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor I,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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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 |
27
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pubmed:volume |
416
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
307-11
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:9373175-Alanine,
pubmed-meshheading:9373175-Amino Acid Sequence,
pubmed-meshheading:9373175-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:9373175-Cell Line,
pubmed-meshheading:9373175-Glycogen Synthase Kinase 3,
pubmed-meshheading:9373175-Glycogen Synthase Kinases,
pubmed-meshheading:9373175-Humans,
pubmed-meshheading:9373175-Insulin,
pubmed-meshheading:9373175-Insulin-Like Growth Factor I,
pubmed-meshheading:9373175-Isoenzymes,
pubmed-meshheading:9373175-Mutagenesis, Site-Directed,
pubmed-meshheading:9373175-Phosphoprotein Phosphatases,
pubmed-meshheading:9373175-Phosphorylation,
pubmed-meshheading:9373175-Phosphoserine,
pubmed-meshheading:9373175-Phosphotyrosine,
pubmed-meshheading:9373175-Protein-Serine-Threonine Kinases,
pubmed-meshheading:9373175-Recombinant Proteins,
pubmed-meshheading:9373175-Serine,
pubmed-meshheading:9373175-Transfection,
pubmed-meshheading:9373175-Tyrosine
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pubmed:year |
1997
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pubmed:articleTitle |
Further evidence that the inhibition of glycogen synthase kinase-3beta by IGF-1 is mediated by PDK1/PKB-induced phosphorylation of Ser-9 and not by dephosphorylation of Tyr-216.
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pubmed:affiliation |
Department of Biochemistry, University of Dundee, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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