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MBC in Press, published online ahead of print March 7, 2007
Mol. Biol. Cell 10.1091/mbc.E06-11-1000

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Submitted on November 9, 2006
Revised on January 26, 2007
Accepted on February 21, 2007

Ent3p and Ent5p Exhibit Cargo-specific Functions in Trafficking Proteins between the Trans-Golgi Network and the Endosomes in Yeast 3

Alenka Copic,*{dagger} Trevor Starr,*{ddagger} and Randy Schekman*

*Howard Hughes Medical Institute and Department of Molecular and Cell Biology, and {ddagger}Graduate Group in Microbiology, University of California at Berkeley, Berkeley, CA 94720

Monitoring Editor: Sandra Lemmon

The phosphoinositide-binding proteins Ent3p and Ent5p are required for protein transport from the trans-Golgi network (TGN) to the vacuole in S. cerevisiae. Both proteins interact with the monomeric clathrin adaptor Gga2p, but Ent5p also interacts with the clathrin adaptor protein complex 1 (AP-1), which facilitates retention of proteins such as Chs3p at the TGN. When both ENT3 and ENT5 are mutated, Chs3p is diverted from an intracellular reservoir to the cell surface. However, Ent3p and Ent5p are not required for the function of AP-1 but rather seem to act in parallel with AP-1 to retain proteins such as Chs3p at the TGN. They have all the properties of clathrin adaptors because they can both bind to clathrin and to cargo proteins. Like AP-1, Ent5p binds to Chs3p, whereas Ent3p facilitates the interaction between Gga2p and the endosomal t-SNARE Pep12p. Thus, Ent3p has an additional function in Gga-dependent transport to the late endosome. Ent3p also facilitates the association between Gga2p and clathrin; however, Ent5p can partially substitute for this function. We conclude that the clathrin adaptors AP-1, Ent3p, Ent5p and the Ggas cooperate in different ways to sort proteins between the TGN and the endosomes.

{dagger}Present address: Department of Biological Sciences, Columbia University, New York, NY 10027.

Address correspondence to: Randy Schekman (schekman{at}berkeley.edu)




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