期刊
DEVELOPMENTAL CELL
卷 43, 期 4, 页码 522-+出版社
CELL PRESS
DOI: 10.1016/j.devcel.2017.10.019
关键词
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资金
- Swiss National Science Foundation [PZ00P3_148269]
- German Research Foundation (DFG) [SFB958/A07]
- Swiss National Science Foundation (SNF) [PZ00P3_148269] Funding Source: Swiss National Science Foundation (SNF)
Clathrin-mediated endocytosis occurs by bending and remodeling of the membrane underneath the coat. Bin-amphiphysin-rvs (BAR) domain proteins are crucial for endocytic membrane remodeling, but how their activity is spatiotemporally controlled is largely unknown. We demonstrate that the membrane remodeling activity of sorting nexin 9 (SNX9), a late-acting endocytic PX-BAR domain protein required for constriction of U-shaped endocytic intermediates, is controlled by an allosteric structural switch involving coincident detection of the clathrin adaptor AP2 and phosphatidylinositol-3,4-bisphosphate (PI(3,4)P-2) at endocytic sites. Structural, biochemical, and cell biological data show that SNX9 is autoinhibited in solution. Binding to PI(3,4) P-2 via its PX-BAR domain, and concomitant association with AP2 via sequences in the linker region, releases SNX9 autoinhibitory contacts to enable membrane constriction. Our results reveal a mechanism for restricting the latent membrane remodeling activity of BAR domain proteins to allow spatiotemporal coupling of membrane constriction to the progression of the endocytic pathway.
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