期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 279, 期 52, 页码 54872-54880出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M409995200
关键词
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Synaptotagmin is a multifunctional membrane protein that may regulate exo-endocytic cycling of synaptic vesicles at the presynaptic plasmalemma. Its C2B domain has been postulated to interact with a variety of effector molecules including acidic phospholipids, phosphoinositides, SNAREs ( soluble N-ethylmaleimide- sensitive factor attachment protein receptors), calcium channels, and the clathrin adaptor complex AP-2. Here we report that a basic motif within the C2B domain is required and sufficient for binding to AP-2 via its mu2 subunit and that this interaction is dependent on multimerization of the AP-2 binding site. Moreover, we show that upon fusion to a plasma membrane reporter protein this sequence is sufficient to target the chimeric molecule for internalization. We hypothesize that basic motifs within multimeric membrane proteins may represent a novel type of clathrin/AP-2-dependent endocytosis signal.
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