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rdf:type |
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lifeskim:mentions |
umls-concept:C0040715,
umls-concept:C0086168,
umls-concept:C0118975,
umls-concept:C0205147,
umls-concept:C0596901,
umls-concept:C0599718,
umls-concept:C0599813,
umls-concept:C0599893,
umls-concept:C1334043,
umls-concept:C1514873,
umls-concept:C1522702,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1879547,
umls-concept:C2697616
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pubmed:issue |
7
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pubmed:dateCreated |
2003-2-10
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pubmed:abstractText |
Small G proteins of the Rho/Rac/Cdc42 family are associated with lipid membranes through their prenylated C termini. Alternatively, these proteins form soluble complexes with GDI proteins. To assess how this membrane partitioning influences the activation of Rac by guanine nucleotide exchange factors, GDP-to-GTP exchange reactions were performed in the presence of liposomes using different forms of Rac-GDP. We show that both non-prenylated Rac-GDP and the soluble complex between prenylated Rac-GDP and GDI are poorly activated by the Dbl homology-pleckstrin homology (DH-PH) domain of the exchange factor Tiam1, whereas prenylated Rac-GDP bound to liposomes is activated about 10 times more rapidly. Sedimentation experiments with liposomes reveal that the DH-PH region of Tiam1 forms, with nucleotide-free prenylated Rac, a membrane-bound complex from which GDI is excluded. Taken together, these experiments demonstrate that the dissociation of Rac-GDP from GDI and its translocation to membrane lipids favor DH-PH-catalyzed nucleotide exchange because the steric hindrance caused by GDI is relieved and because the membrane environment favors functional interaction between the DH-PH domain and the small G protein.
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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/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Dissociation...,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/MCF2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Retroviridae Proteins, Oncogenic,
http://linkedlifedata.com/resource/pubmed/chemical/TIAM1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/platelet protein P47,
http://linkedlifedata.com/resource/pubmed/chemical/rac GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rho GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rho guanine nucleotide...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4756-62
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12471028-Blood Proteins,
pubmed-meshheading:12471028-Gene Expression Regulation,
pubmed-meshheading:12471028-Guanine Nucleotide Dissociation Inhibitors,
pubmed-meshheading:12471028-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:12471028-Humans,
pubmed-meshheading:12471028-Liposomes,
pubmed-meshheading:12471028-Phosphoproteins,
pubmed-meshheading:12471028-Protein Structure, Tertiary,
pubmed-meshheading:12471028-Protein Transport,
pubmed-meshheading:12471028-Proteins,
pubmed-meshheading:12471028-Proto-Oncogene Proteins,
pubmed-meshheading:12471028-Retroviridae Proteins, Oncogenic,
pubmed-meshheading:12471028-Saccharomyces cerevisiae,
pubmed-meshheading:12471028-Sequence Homology,
pubmed-meshheading:12471028-Signal Transduction,
pubmed-meshheading:12471028-Transfection,
pubmed-meshheading:12471028-rac GTP-Binding Proteins,
pubmed-meshheading:12471028-rho GTP-Binding Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
Dissociation of GDP dissociation inhibitor and membrane translocation are required for efficient activation of Rac by the Dbl homology-pleckstrin homology region of Tiam.
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pubmed:affiliation |
CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, 660 Route des Lucioles, 06560 Valbonne, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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