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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
2005-5-30
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pubmed:abstractText |
The small GTP-binding protein ADP-ribosylation factor 6 (Arf6) is involved in plasma membrane/endosomes trafficking. However, precisely how the activation of Arf6 regulates vesicular transport is still unclear. Here, we show that, in vitro, recombinant Arf6GTP recruits purified clathrin-adaptor complex AP-2 (but not AP-1) onto phospholipid liposomes in the absence of phosphoinositides. We also show that phosphoinositides and Arf6 tightly cooperate to translocate AP-2 to the membrane. In vivo, Arf6GTP (but not Arf6GDP) was found associated to AP-2. The expression of the GTP-locked mutant of Arf6 leads to the plasma membrane redistribution of AP-2 in Arf6GTP-enriched areas. Finally, we demonstrated that the expression of the GTP-locked mutant of Arf6 inhibits transferrin receptor internalization without affecting its recycling. Altogether, our results demonstrated that Arf6GTP interacts specifically with AP-2 and promotes its membrane recruitment. These findings strongly suggest that Arf6 plays a major role in clathrin-mediated endocytosis by directly controlling the assembly of the AP-2/clathrin coat.
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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/ADP-Ribosylation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/ADP-ribosylation factor 6,
http://linkedlifedata.com/resource/pubmed/chemical/Clathrin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Transferrin,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor AP-2,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Transferrin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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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 |
3
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21661-6
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15802264-ADP-Ribosylation Factors,
pubmed-meshheading:15802264-Animals,
pubmed-meshheading:15802264-Brain,
pubmed-meshheading:15802264-Cell Membrane,
pubmed-meshheading:15802264-Clathrin,
pubmed-meshheading:15802264-Cricetinae,
pubmed-meshheading:15802264-DNA-Binding Proteins,
pubmed-meshheading:15802264-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:15802264-Endocytosis,
pubmed-meshheading:15802264-Glutathione Transferase,
pubmed-meshheading:15802264-Guanosine Triphosphate,
pubmed-meshheading:15802264-HeLa Cells,
pubmed-meshheading:15802264-Humans,
pubmed-meshheading:15802264-Immunoprecipitation,
pubmed-meshheading:15802264-Kinetics,
pubmed-meshheading:15802264-Liposomes,
pubmed-meshheading:15802264-Microscopy, Confocal,
pubmed-meshheading:15802264-Mutation,
pubmed-meshheading:15802264-Phosphatidylinositols,
pubmed-meshheading:15802264-Protein Binding,
pubmed-meshheading:15802264-Protein Transport,
pubmed-meshheading:15802264-Receptors, Transferrin,
pubmed-meshheading:15802264-Time Factors,
pubmed-meshheading:15802264-Transcription Factor AP-2,
pubmed-meshheading:15802264-Transcription Factors,
pubmed-meshheading:15802264-Transfection,
pubmed-meshheading:15802264-Transferrin
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pubmed:year |
2005
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pubmed:articleTitle |
The small G-protein Arf6GTP recruits the AP-2 adaptor complex to membranes.
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pubmed:affiliation |
Institut de Pharmacologie Moleculaire et Cellulaire, CNRS-Unité Mixte de Recherche 6097, 660 Route des Lucioles, 06560 Valbonne Sophia-Antipolis, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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