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MBC in Press, published online ahead of print June 21, 2006
Mol. Biol. Cell 10.1091/mbc.E06-05-0410

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Submitted on May 11, 2006
Revised on June 12, 2006
Accepted on June 14, 2006

Distinct Roles for TGN/Endosome Epsin-like Adaptors Ent3p and Ent5p

Giancarlo Costaguta,* Mara C. Duncan,* G. Esteban Fernández,* Grace H. Huang,{dagger} and Gregory S. Payne*

*Department of Biological Chemistry, David Geffen School of Medicine and {dagger}Department of Biostatistics, School of Public Health, UCLA, Los Angeles, CA 90095

Monitoring Editor: Janet Shaw

Clathrin adaptors are key factors in clathrin-coated vesicle formation, coupling clathrin to cargo and/or the lipid bilayer. A physically-interacting network of three classes of adaptors participate in clathrin-mediated traffic between the trans-Golgi network (TGN) and endosomes: AP-1, Gga proteins, and epsin-like proteins. Here we investigate functional relationships within this network through transport assays and protein localization analysis in living yeast cells. We observed that epsin-like protein Ent3p preferentially localized with Gga2p whereas Ent5p distributed equally between AP-1 and Gga2p. Ent3p was mislocalized in Gga-deficient but not in AP-1-deficient cells. In contrast, Ent5p retained localization in cells lacking either or both AP-1 and Gga proteins. The Ent proteins were dispensable for AP-1 or Gga localization. Synthetic genetic growth and {alpha}-factor maturation defects were observed when ent5{Delta} but not ent3{Delta} was introduced together with deletions of the GGA genes. In AP-1-deficient cells, ent3{Delta} and to a lesser extent ent5{Delta} caused minor {alpha}-factor maturation defects, but together resulted in a near-lethal phenotype. Deletions of ENT3 and ENT5 also displayed synthetic defects similar to, but less severe than, synthetic effects of AP-1 and Gga inactivation. These results differentiate Ent3p and Ent5p function in vivo, suggesting that Ent3p acts primarily with Gga proteins whereas Ent5p acts with both AP-1 and Gga proteins but is more critical for AP-1-mediated transport. The data also support a model in which the Ent adaptors provide important accessory functions to AP-1 and Gga proteins in TGN/endosome traffic.

Address correspondence to: Gregory S. Payne (gpayne{at}mednet.ucla.edu)




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