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Vol. 14, Issue 2, 625-641, February 2003
and
*University of Cambridge, Department of Clinical
Biochemistry, Cambridge Institute for Medical Research, Cambridge CB2
2XY, United Kingdom; and We have used GST pulldowns from A431 cell cytosol to identify three
new binding partners for the MRC Laboratory of
Molecular Biology, Cambridge CB2 2QH, United Kingdom
-adaptin appendage: Snx9, ARF GAP1, and
a novel ENTH domain-containing protein, epsinR. EpsinR is a highly
conserved protein that colocalizes with AP-1 and is enriched in
purified clathrin-coated vesicles. However, it does not require AP-1 to
get onto membranes and remains membrane-associated in AP-1-deficient
cells. Moreover, although epsinR binds AP-1 via its COOH-terminal
domain, its NH2-terminal ENTH domain can be independently
recruited onto membranes, both in vivo and in vitro. Brefeldin A causes
epsinR to redistribute into the cytosol, and recruitment of the ENTH
domain requires GTPS, indicating that membrane association is ARF
dependent. In protein-lipid overlay assays, the epsinR ENTH domain
binds to PtdIns(4)P, suggesting a possible mechanism for ARF-dependent
recruitment onto TGN membranes. When epsinR is depleted from cells by
RNAi, cathepsin D is still correctly processed intracellularly to the
mature form. This indicates that although epsinR is likely to be an
important component of the AP-1 network, it is not necessary for the
sorting of lysosomal enzymes.
Online
version of this article contains video material. Online version is
available at www.molbiolcell.org.
Corresponding author. E-mail address:
msr12{at}mole.bio.cam.ac.uk.
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