Source:http://linkedlifedata.com/resource/pubmed/id/12102558
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2002-7-9
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pubmed:abstractText |
GTPases of the Ras subfamily regulate a diverse array of cellular-signaling pathways, coupling extracellular signals to the intracellular response machinery. Guanine nucleotide exchange factors (GEFs) are primarily responsible for linking cell-surface receptors to Ras protein activation. They do this by catalyzing the dissociation of GDP from the inactive Ras proteins. GTP can then bind and induce a conformational change that permits interaction with downstream effectors. Over the past 5 years, approximately 20 novel Ras-family GEFs have been identified and characterized. These data indicate that a variety of different signaling mechanisms can be induced to activate Ras, enabling tyrosine kinases, G-protein-coupled receptors, adhesion molecules, second messengers, and various protein-interaction modules to relocate and/or activate GEFs and elevate intracellular Ras-GTP levels. This review discusses the structure and function of the catalytic or CDC25 homology domain common to almost all Ras-family GEFs. It also details our current knowledge about the regulation and function of this rapidly growing family of enzymes that include Sos1 and 2, GRF1 and 2, CalDAG-GEF/GRP1-4, C3G, cAMP-GEF/Epac 1 and 2, PDZ-GEFs, MR-GEF, RalGDS family members, RalGPS, BCAR3, Smg GDS, and phospholipase C(epsilon).
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0079-6603
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
71
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
391-444
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12102558-Amino Acid Sequence,
pubmed-meshheading:12102558-Animals,
pubmed-meshheading:12102558-Enzyme Activation,
pubmed-meshheading:12102558-Humans,
pubmed-meshheading:12102558-Molecular Sequence Data,
pubmed-meshheading:12102558-Neoplasms,
pubmed-meshheading:12102558-Protein Structure, Tertiary,
pubmed-meshheading:12102558-Sequence Homology, Amino Acid,
pubmed-meshheading:12102558-ras GTPase-Activating Proteins,
pubmed-meshheading:12102558-ras Guanine Nucleotide Exchange Factors,
pubmed-meshheading:12102558-ras Proteins,
pubmed-meshheading:12102558-ras-GRF1
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pubmed:year |
2002
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pubmed:articleTitle |
A growing family of guanine nucleotide exchange factors is responsible for activation of Ras-family GTPases.
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pubmed:affiliation |
Department of Biochemistry and Molecular, Biology and Walther Oncology Center, Indiana University School of Medicine, Indianapolis 46202, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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