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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 Peteraa 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
, 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, while overexpression of an active form of Ypt6p partially suppresses the recycling defect of rcy1 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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