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PMID:15537705
Citation |
Chen, SH, Chen, S, Tokarev, AA, Liu, F, Jedd, G and Segev, N (2005) Ypt31/32 GTPases and their novel F-box effector protein Rcy1 regulate protein recycling. Mol. Biol. Cell 16:178-92 |
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Abstract |
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 regulates 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 regulate the recycling of the furin-homolog Kex2 to the Golgi. Therefore, Ypt31/32 and Rcy1 mediate endosome-to-Golgi transport, because 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. |
Links |
PubMed PMC539162 Online version:10.1091/mbc.E04-03-0258 |
Keywords |
Blotting, Western; Endosomes/metabolism; F-Box Proteins; Glutathione Transferase/metabolism; Golgi Apparatus/metabolism; Membrane Proteins/metabolism; Microscopy, Fluorescence; Models, Biological; Phosphorylation; Plasmids/metabolism; Proprotein Convertases/metabolism; Protein Binding; Protein Processing, Post-Translational; Protein Structure, Tertiary; R-SNARE Proteins; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/metabolism; Saccharomyces cerevisiae Proteins/physiology; Subcellular Fractions; Temperature; Two-Hybrid System Techniques; Ubiquitin/metabolism; Vesicular Transport Proteins; rab GTP-Binding Proteins/physiology |
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