The small G-protein Arf6GTP recruits the AP-2 adaptor complex to membranes |
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Authors: | Paleotti Olivia Macia Eric Luton Frederic Klein Stephanie Partisani Mariagrazia Chardin Pierre Kirchhausen Tom Franco Michel |
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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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Abstract: | 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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