A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals

被引:353
作者
David, C
McPherson, PS
Mundigl, O
DeCamilli, P
机构
[1] YALE UNIV,SCH MED,BOYER CTR MOLEC MED,DEPT CELL BIOL,NEW HAVEN,CT 06510
[2] YALE UNIV,SCH MED,HOWARD HUGHES MED INST,NEW HAVEN,CT 06510
关键词
SH3; domain; adaptin; Grb; 2; clathrin; RVS genes;
D O I
10.1073/pnas.93.1.331
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Amphiphysin, a major autoantigen in paraneoplastic Stiff-Man syndrome, is an SH3 domain-containing neuronal protein, concentrated in nerve terminals, Here, we demonstrate a specific, SH3 domain-mediated, interaction between amphiphysin and dynamin by gel overlay and affinity chromatography, In addition, we show that the two proteins are colocalized in nerve terminals and are coprecipitated from brain extracts consistent with their interactions in situ, We also report that a region of amphiphysin distinct from its SH3 domain mediates its binding to the cr,subunit of AP2 adaptin, which is also concentrated in nerve terminals, These findings support a role of amphiphysin in synaptic vesicle endocytosis.
引用
收藏
页码:331 / 335
页数:5
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