Gamma-synergin: an EH domain-containing protein that interacts with gamma-adaptin.
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 gamma-adaptin subunit of the AP-1 complex as bait. Two novel, ubiquitously expressed proteins were found: p34, which interacts with both gamma-adaptin and alpha-adaptin, and gamma-synergin, an alternatively spliced protein with an apparent molecular mass of approximately 110-190 kD, which only interacts with gamma-adaptin. gamma-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 gamma-adaptin and it contains an Eps15 homology (EH) domain, although the EH domain is not part of the gamma-adaptin binding site. In cells expressing alpha-adaptin with the gamma-adaptin ear, a construct that goes mainly to the plasma membrane, much of the gamma-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 gamma-synergin links the AP-1 complex to another protein or proteins.
Mesh Terms:
Adaptor Protein Complex alpha Subunits, Adaptor Protein Complex gamma Subunits, Adaptor Proteins, Vesicular Transport, Alternative Splicing, Animals, Binding Sites, Brain, Carrier Proteins, Cell Line, Cell Membrane, Cloning, Molecular, Cytosol, Dogs, Drosophila Proteins, Golgi Apparatus, Intracellular Membranes, Liver, Membrane Proteins, Mice, Microtubule-Associated Proteins, Molecular Sequence Data, Molecular Weight, RNA, Messenger, Rats, Recombinant Fusion Proteins, Sequence Deletion, Yeasts
Adaptor Protein Complex alpha Subunits, Adaptor Protein Complex gamma Subunits, Adaptor Proteins, Vesicular Transport, Alternative Splicing, Animals, Binding Sites, Brain, Carrier Proteins, Cell Line, Cell Membrane, Cloning, Molecular, Cytosol, Dogs, Drosophila Proteins, Golgi Apparatus, Intracellular Membranes, Liver, Membrane Proteins, Mice, Microtubule-Associated Proteins, Molecular Sequence Data, Molecular Weight, RNA, Messenger, Rats, Recombinant Fusion Proteins, Sequence Deletion, Yeasts
J. Cell Biol.
Date: Sep. 06, 1999
PubMed ID: 10477754
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