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MBC in Press, published online ahead of print March 26, 2008
Mol. Biol. Cell 10.1091/mbc.E08-01-0068

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Submitted on January 23, 2008
Revised on March 12, 2008
Accepted on March 18, 2008

Ear1p and Ssh4p Are New Adaptors of the Ubiquitin Ligase Rsp5p for Cargo Ubiquitylation and Sorting at Multivesicular Bodies

Sébastien Léon, Zoi Erpapazoglou, and Rosine Haguenauer-Tsapis

Institut Jacques Monod, UMR 7592 CNRS, Universités Paris 6 et 7, Paris, France

Monitoring Editor: Sandra Lemmon

The ubiquitylation of membrane proteins destined for the the vacuole/lysosome is essential for their recognition by the endosomal sorting machinery and their internalization into vesicles of multivesicular bodies (MVBs). In yeast, this process requires Rsp5p, an essential ubiquitin ligase of the Nedd4 family. We describe here two redundant proteins, Ear1p and Ssh4p, required for the vacuolar targeting of several cargoes originating from the Golgi or the plasma membrane. Ear1p is an endosomal protein that interacts with Rsp5p through its PPxY motifs and is required for the ubiquitylation of selected cargoes before their MVB sorting. In-frame fusion of cargo to ubiquitin overcomes the need for Ear1p/Ssh4p, confirming a role for these proteins in cargo ubiquitylation. Interestingly, Ear1p is itself ubiquitylated by Rsp5p and targeted to the vacuole. Finally, Ear1p overexpression leads to Rsp5p accumulation at endosomes, interfering with some of its functions in trafficking. Therefore, Ear1p/Ssh4p recruit Rsp5p and assist it in its function at MVBs by directing the ubiquitylation of specific cargoes.

Address correspondence to: Sébastien Léon (leon{at}ijm.jussieu.fr)






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