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A more recent version of this article appeared on January 1, 2005
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Submitted on March 26, 2004
Revised on October 7, 2004
Accepted on October 26, 2004
Department of Biological Sciences, Laboratory for Molecular Biology, University of Illinois at Chicago, Chicago, IL 60612
Monitoring Editor: Vivek Malhotra
Ypt/Rab GTPases control various aspects of vesicle formation and targeting via their diverse effectors. We report a new role for these GTPases in protein recycling through a novel effector. The F-box protein, Rcy1, which mediates plasma membrane recycling, is identified here as a downstream effector of the Ypt31/32 GTPase pair because it binds active GTP-bound Ypt31/32 and colocalizes with these GTPases on late Golgi and endosomes. Furthermore, Ypt31/32 regulate the polarized localization and half-life of Rcy1. This suggests that Ypt/Rabs can regulate the protein level of their effectors, in addition to the established ways by which they control their effectors. We show that like Rcy1, Ypt31/32 regulate the coupled phosphorylation and recycling of the plasma-membrane v-SNARE, Snc1. Moreover, Ypt31/32 and Rcy1 also regulate the recycling of the furin-homolog Kex2 to the Golgi. Therefore, Ypt31/32 and Rcy1 mediate endosome-to-Golgi transport, as this is the only step shared by Snc1 and Kex2. Finally, we show that Rcy1 physically interacts with Snc1. Based on this result and because F-box proteins serve as adaptors between specific substrates and ubiquitin ligases, we propose that Ypt31/32 GTPases regulate the function of Rcy1 in the phosphorylation and/or ubiquitination of proteins that recycle through the Golgi.
Feinberg School of Medicine, Northwestern University, Chicago, IL 60611; Department of Biological Sciences, Illinois State University, Normal, IL 61790; The Rockefeller University, New York, NY 10021.
||Corresponding author.
E-mail: nava{at}uic.edu
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