Clathrin interacts specifically with amphiphysin and is displaced by dynamin

FEBS Letters

McMahon, Harvey T¹  Wigge, Patrick¹  Smith, Corrin¹ 

[1] Neurobiology Division, MRC-LMB, Cambridge CB2 2QH, UK

关键词: Amphiphysin;    Clathrin;    Coated pit;    Dynamin;    Synaptic vesicle Endocytosis;    AP-2;    adaptor protein complex 2;    Amph;    amphiphysin;    GST;    glutathione-S-transferase;    GTP;    guanosine triphosphate;    PAGE;    polyacrylamide gel electrophoresis;    SH3;    src-homology 3;   

DOI  :  10.1016/S0014-5793(97)00928-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Amphiphysin is an SH3 domain protein that has been implicated in synaptic vesicle endocytosis. We have recently cloned a second amphiphysin isoform, Amph2 (sequence submitted to GenBank, Y13380). Proteins capable of forming a complex with amphiphysin were isolated from rat brain by using recombinant GST-Amph2 for binding experiments. As well as interacting with dynamin I, the full-length protein bound to a weaker 180-kDa band. Immunoblotting demonstrated this protein to be clathrin. To address whether this is a direct interaction, the clathrin binding to amphiphysin was reconstituted in vitro with purified proteins. The N-terminal domain of Amph2 is sufficient for clathrin binding. Dynamin, which interacts with the SH3 domain of Amph2, displaces clathrin from the N-terminus. We propose a model that may explain how clathrin and dynamin are recruited to non-overlapping sites of the coated pit.

【 授权许可】

Unknown