Two distinct interaction motifs in amphiphysin bind two independent sites on the clathrin terminal domain β-propeller

被引:94
作者
Miele, AE
Watson, PJ
Evans, PR
Traub, LM [1 ]
Owen, DJ
机构
[1] Univ Pittsburgh, Sch Med, Dept Cell Biol & Physiol, Pittsburgh, PA 15261 USA
[2] MRC, Mol Biol Lab, Cambridge CB2 2QH, England
[3] Univ Cambridge, Cambridge Inst Med Res, Cambridge CB2 2XY, England
关键词
D O I
10.1038/nsmb736
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
During the assembly of clathrin-coated vesicles, many peripheral membrane proteins, including the amphiphysins, use LLDLD-type clathrin-box motifs to interact with the N-terminal beta-propeller domain (TD) of clathrin. The 2.3 Angstrom resolution structure of the clathrin TD in complex with a TLPWDLWTT peptide from amphiphysin 1 delineates a second clathrin-binding motif, PWXXW ( the W box), that binds at a site on the TD remote from the clathrin box binding site. The presence of both sequence motifs within the unstructured region of the amphiphysins allows them to bind more tightly to free TDs than do other endocytic proteins that contain only clathrin-box motifs. This property, along with the propensity of the N-terminal BAR domain to bind curved membranes, will preferentially localize amphiphysin and its partner, dynamin, to the periphery of invaginated clathrin lattices.
引用
收藏
页码:242 / 248
页数:7
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