Clathrin adaptors. AP2 controls clathrin polymerization with a membrane-activated switch.
Clathrin adaptors. AP2 controls clathrin polymerization with a membrane-activated switch.
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DOI：
10.1126/science.1254836
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发表时间：
2014-07-25
期刊：
影响因子：
--
通讯作者：
Owen DJ
中科院分区：
文献类型：
--
作者：
Kelly BT;Graham SC;Liska N;Dannhauser PN;Höning S;Ungewickell EJ;Owen DJ
Clathrin-mediated endocytosis (CME) is vital for the internalization of most cell-surface proteins. In CME, plasma membrane-binding clathrin adaptors recruit and polymerize clathrin to form clathrin-coated ‘pits’ into which cargo is sorted. AP2 is the most abundant adaptor, and is pivotal to CME. By determining a new structure of AP2 that includes the clathrin-binding β2-hinge and developing an AP2-dependent budding assay, we reveal the existence of an autoinhibitory mechanism that prevents clathrin recruitment by cytosolic AP2. A large-scale conformational change driven by the plasma membrane phosphoinositide PtdIns(4,5)P2 and cargo relieves this autoinhibition, so triggering clathrin recruitment and hence clathrin-coated bud formation. This molecular switching mechanism constitutes an unsuspected layer of regulation that couples AP2’s membrane recruitment to its key functions of cargo and clathrin binding.
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涂有网状蛋白涂层坑的前五秒钟。
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