期刊
CURRENT BIOLOGY
卷 21, 期 7, 页码 574-579出版社
CELL PRESS
DOI: 10.1016/j.cub.2011.02.034
关键词
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资金
- Association pour la Recherche contre le Cancer [SL220100601356]
- Agence Nationale pour la Recherche [ANR-08-BLAN-0111]
- Institut Curie
- CNRS
- Biotechnology and Biological Sciences Research Council [BBS/B/04072] Funding Source: researchfish
- Agence Nationale de la Recherche (ANR) [ANR-08-BLAN-0111] Funding Source: Agence Nationale de la Recherche (ANR)
The small GTP-binding protein ADP-ribosylation factor 6 (ARF6) controls the endocytic recycling pathway of several plasma membrane receptors. We analyzed the localization and GDP/GTP cycle of GFP-tagged ARF6 by total internal reflection fluorescent microscopy. We found that ARF6-GFP associates with clathrin-coated pits (CCPs) at the plasma membrane in a GTP-dependent manner in a mechanism requiring the adaptor protein complex AP-2. In CCP, GTP-ARF6 mediates the recruitment of the ARF-binding domain of downstream effectors including JNK-interacting proteins 3 and 4 (JIP3 and JIP4) after the burst recruitment of the clathrin uncoating component auxilin. ARF6 does not contribute to receptor-mediated clathrin-dependent endocytosis. In contrast, we found that interaction of ARF6 and JIPs on endocytic vesicles is required for trafficking of the transferrin receptor in the fast, microtubule-dependent endocytic recycling pathway. Our findings unravel a novel mechanism of separation of ARF6 activation and effector function, ensuring that fast recycling may be determined at the level of receptor incorporation into CCPs.
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