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Originally published as MBC in Press, 10.1091/mbc.E04-12-1077 on March 9, 2005

Vol. 16, Issue 5, 2554-2565, May 2005

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The Aftiphilin/p200/{gamma}-Synergin Complex

Jennifer Hirst, Georg H.H. Borner, Michael Harbour, and Margaret S. Robinson

Department of Clinical Biochemistry, Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 2XY, United Kingdom

Submitted December 14, 2004; Revised February 11, 2005; Accepted February 24, 2005
Monitoring Editor: Sandra Schmid

Aftiphilin is a protein that was recently identified in database searches for proteins with motifs that interact with AP-1 and clathrin, but its function is unknown. Here we demonstrate that aftiphilin has a second, atypical clathrin binding site, YQW, that colocalizes with AP-1 by immunofluorescence, and that is enriched in clathrin-coated vesicles (CCVs), confirming that it is a bona fide component of the CCV machinery. By gel filtration, aftiphilin coelutes with two other AP-1 binding partners, p200a and {gamma}-synergin. Antibodies against any one of these three proteins immunoprecipitate the other two, and knocking down any of the three proteins by siRNA causes a reduction in the levels of the other two, indicating that they form a stable complex. Like AP-1–depleted cells, aftiphilin-depleted cells missort a CD8-furin chimera and the lysosomal enzyme cathepsin D. However, whereas AP-1–depleted cells recycle endocytosed transferrin more slowly than untreated cells, aftiphilin-depleted cells accumulate endocytosed transferrin in a peripheral compartment and recycle it more rapidly. These observations show that in general, the aftiphilin/p200/{gamma}-synergin complex facilitates AP-1 function, but the complex may have additional functions as well, because of the opposing effects of the two knockdowns on transferrin recycling.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E04-12-1077) on March 9, 2005.

Address correspondence to: Margaret S. Robinson (msr12{at}mole.bio.cam.ac.uk).




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