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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6458
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pubmed:dateCreated |
1994-3-21
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pubmed:databankReference |
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pubmed:abstractText |
A new brain serine/threonine protein kinase may be a target for the p21ras-related proteins Cdc42 and Rac1. The kinase sequence is related to that of the yeast protein STE20, implicated in pheromone-response pathways. The kinase complexes specifically with activated (GTP-bound) p21, inhibiting p21 GTPase activity and leading to kinase autophosphorylation and activation. Autophosphorylated kinase has a decreased affinity for Cdc42/Rac, freeing the p21 for further stimulatory activities or downregulation by GTPase-activating proteins. This bimolecular interaction provides a model for studying p21 regulation of mammalian phosphorylation signalling pathways.
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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/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/STE20 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rac GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rho GTP-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
367
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
40-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8107774-Amino Acid Sequence,
pubmed-meshheading:8107774-Animals,
pubmed-meshheading:8107774-Brain,
pubmed-meshheading:8107774-Cattle,
pubmed-meshheading:8107774-Enzyme Activation,
pubmed-meshheading:8107774-GTP Phosphohydrolases,
pubmed-meshheading:8107774-GTP-Binding Proteins,
pubmed-meshheading:8107774-Guanosine Diphosphate,
pubmed-meshheading:8107774-Guanosine Triphosphate,
pubmed-meshheading:8107774-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:8107774-Molecular Sequence Data,
pubmed-meshheading:8107774-Phosphorylation,
pubmed-meshheading:8107774-Protein Binding,
pubmed-meshheading:8107774-Protein-Serine-Threonine Kinases,
pubmed-meshheading:8107774-Protein-Tyrosine Kinases,
pubmed-meshheading:8107774-Rats,
pubmed-meshheading:8107774-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8107774-Sequence Homology, Amino Acid,
pubmed-meshheading:8107774-Signal Transduction,
pubmed-meshheading:8107774-p21-Activated Kinases,
pubmed-meshheading:8107774-rac GTP-Binding Proteins,
pubmed-meshheading:8107774-rho GTP-Binding Proteins
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pubmed:year |
1994
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pubmed:articleTitle |
A brain serine/threonine protein kinase activated by Cdc42 and Rac1.
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pubmed:affiliation |
Institute of Molecular & Cell Biology, National University of Singapore, Kent Ridge.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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