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-Synergin: An EH Domain–containing Protein that Interacts with -Adaptin
Correspondence to: Margaret S. Robinson, University of Cambridge, CIMR, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2XY, England. Tel:44-1223-330163 Fax:44-1223-762322 E-mail:msr12{at}mole.bio.cam.ac.uk.
The AP-1 adaptor complex is associated with the TGN, where it links selected membrane proteins to the clathrin lattice, enabling these proteins to be concentrated in clathrin-coated vesicles. To identify other proteins that participate in the clathrin-coated vesicle cycle at the TGN, we have carried out a yeast two- hybrid library screen using the -adaptin subunit of the AP-1 complex as bait. Two novel, ubiquitously expressed proteins were found: p34, which interacts with both -adaptin and 
-adaptin, and -synergin, an alternatively spliced protein with an apparent molecular mass of ~110–190 kD, which only interacts with -adaptin. -Synergin is associated with AP-1 both in the cytosol and on TGN membranes, and it is strongly enriched in clathrin-coated vesicles. It binds directly to the ear domain of -adaptin and it contains an Eps15 homology (EH) domain, although the EH domain is not part of the -adaptin binding site. In cells expressing -adaptin with the -adaptin ear, a construct that goes mainly to the plasma membrane, much of the -synergin is also rerouted to the plasma membrane, indicating that it follows AP-1 onto membranes rather than leading it there. The presence of an EH domain suggests that -synergin links the AP-1 complex to another protein or proteins.
Key Words:
AP-1, -adaptin, clathrin, TGN, EH domain
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