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Genetics, Vol. 164, 469-477, June 2003, Copyright © 2003

Opposite Roles of the F-Box Protein Rcy1p and the GTPase-Activating Protein Gyp2p During Recycling of Internalized Proteins in Yeast

Céline Lafourcadea, Jean-Marc Galanb, and Matthias Petera
a Swiss Federal Institute of Technology Zurich (ETH), Institute of Biochemistry, 8093 Zurich, Switzerland
b Institut Jacques Monod-CNRS, 75251 Paris Cedex 05, France

Corresponding author: Matthias Peter, Institute of Biochemistry, ETH Hoenggerberg HPM G 6.2, 8093 Zurich, Switzerland., matthias.peter{at}bc.biol.ethz.ch (E-mail)

Communicating editor: B. J. ANDREWS

The F-box protein Rcy1p is part of a non-SCF (Skp1p-cullin-F-box protein) complex involved in recycling of internalized material. Like rcy1{Delta}, cells lacking the Rab-GTPase Ypt6p or its heterodimeric GEFs Rgp1p and Ric1p are unable to recycle the v-SNARE Snc1p. Here we provide genetic evidence suggesting that Rcy1p is a positive regulator of Ypt6p. Deletion of the GAP Gyp2p restores recycling in rcy1{Delta}, while overexpression of an active form of Ypt6p partially suppresses the recycling defect of rcy1{Delta} cells. Conversely, overexpression of Gyp2p in wild-type cells interferes with recycling of GFP-Snc1p, and the cells accumulate membrane structures as evidenced by electron microscopy. Gyp2p-GFP is distributed throughout the cytoplasm and accumulates in punctate structures, which concentrate in an actin-dependent manner at sites of polarized growth. Taken together, our results suggest that the F-box protein Rcy1p may activate the Ypt6p GTPase module during recycling.




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