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Hsc70‐induced Changes in Clathrin‐Auxilin Cage Structure Suggest a Role for Clathrin Light Chains in Cage Disassembly
Author(s) -
Young Anna,
StoilovaMcPhie Svetla,
Rothnie Alice,
Vallis Yvonne,
HarveySmith Phillip,
Ranson Neil,
Kent Helen,
Brodsky Frances M.,
Pearse Barbara M. F.,
Roseman Alan,
Smith Corinne J.
Publication year - 2013
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12085
Subject(s) - clathrin , biology , microbiology and biotechnology , endocytosis , clathrin adaptor proteins , biophysics , biochemistry , receptor
We have used cryo‐electron microscopy to determine the 3D structure of a complex of clathrin, auxilin401‐910 and Hsc70 trapped early in the recruitment of Hsc70 to the clathrin cage. We observed that Hsc70 bound asymmetrically to the clathrin vertex and induced structural changes close to the location of clathrin light chains on the outermost edge of the cage. Clathrin disassembly assays using light scattering suggested that loss of clathrin light chains reduced the efficiency with which auxilin could facilitate disassembly.