Document Detail


Interaction of amphiphysins with AP-1 clathrin adaptors at the membrane.
MedLine Citation:
PMID:  23190214     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The assembly of clathrin/AP-1-coated vesicles on the trans-Golgi network and endosomes is much less studied than of clathrin/AP-2 vesicles at the plasma membrane for endocytosis. In vitro, AP-1 association to protein-free liposomes had been shown to require phosphoinositides, Arf1•GTP, and additional cytosolic factor(s). We have purified an active fraction from brain cytosol and found it to contain amphiphysin 1 and 2 and endophilin A1, three proteins known to be involved in the formation of AP-2/clathrin coats at the plasma membrane. Assays with bacterially expressed and purified proteins showed AP-1 stabilization on liposomes to depend on amphiphysin 2 or the amphiphysin 1/2 heterodimer. Activity is independent of the SH3 domain, but requires the WDLW motif interacting with γ-adaptin. Endogenous amphiphysin in neurons and transfected protein in cell lines colocalize perinuclearly with AP-1 at the trans-Golgi network. This localization depends on the clathrin and adaptor interaction sequence in the amphiphysins and is sensitive to brefeldin A, which inhibits Arf1-dependent AP-1 recruitment. Interaction between AP-1 and amphiphysin 1/2 in vivo was demonstrated by coimmunoprecipitation after crosslinking. These results suggest an involvement of amphiphysins not only with AP-2 at the plasma membrane, but also in AP-1/clathrin coat formation at the trans-Golgi network.
Authors:
Sonja Huser; Gregor Suri; Pascal Crottet; Martin Spiess
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-11-29
Journal Detail:
Title:  The Biochemical journal     Volume:  -     ISSN:  1470-8728     ISO Abbreviation:  Biochem. J.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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