期刊
NATURE
卷 517, 期 7535, 页码 493-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nature14064
关键词
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资金
- Agence Nationale pour la Recherche [ANR-09-BLAN-283, ANR-10-LBX-0038, ANR-11BSV201403, ANR-12-BSV5-0014]
- Indo-French Centre for the Promotion of Advanced Science [3803]
- Marie Curie Actions - Networks for Initial Training [FP7-PEOPLE-2010-ITN]
- European Research Council [340485]
- Marie Curie International Reintegration Grant [FP7-RG-277078]
- Royal Society [RG120481]
- Fondation ARC pour la Recherche sur le Cancer [DEQ20120323737]
- National Institutes of Health [R01 GM106720]
- La Ligue contre le Cancer, Comite de Paris [RS08/75-89]
- Fondation ARC pour la Recherche sur le Cancer
- AXA Research Funds
- Biological Sciences Research Council
- Chateaubriand fellowship
- France and Chicago Collaborating in the Sciences grant
- Biotechnology and Biological Sciences Research Council [BB/I018921/1] Funding Source: researchfish
- Medical Research Council [MC_U105178795] Funding Source: researchfish
- BBSRC [BB/I018921/1] Funding Source: UKRI
- MRC [MC_U105178795] Funding Source: UKRI
- Agence Nationale de la Recherche (ANR) [ANR-12-BSV5-0014] Funding Source: Agence Nationale de la Recherche (ANR)
During endocytosis, energy is invested to narrow the necks of cargo-containing plasma membrane invaginations to radii at which the opposing segments spontaneously coalesce, thereby leading to the detachment by scission of endocytic uptake carriers'. In the clathrin pathway, dynamin uses mechanical energy from GTP hydrolysis to this effect(2-4), assisted by the BIN/amphiphysin/Rvs (BAR) domain-containing protein endophilin(5,6). Clathrin-independent endocytic events are often less reliant on dynamin(7), and whether in these cases BAR domain proteins such as endophilin contribute to scission has remained unexplored. Here we show, in human and other mammalian cell lines, that endophilin-A2 (endoA2) specifically and functionally associates with very early uptake structures that are induced by the bacterial Shiga and cholera toxins, which are both clathrin-independent endocytic cargoes'. In controlled in vitro systems, endoA2 reshapes membranes before scission. Furthermore, we demonstrate that endoA2, dynamin and actin contribute in parallel to the scission of Shiga-toxin-induced tubules. Our results establish a novel function of endoA2 in clathrin-independent endocytosis. They document that distinct scission factors operate in an additive manner, and predict that specificity within a given uptake process arises from defined combinations of universal modules. Our findings highlight a previously unnoticed link between membrane scaffolding by endoA2 and pulling-force-driven dynamic scission.
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