| pubmed-article:15537705 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15537705 | lifeskim:mentions | umls-concept:C0282114 | lld:lifeskim |
| pubmed-article:15537705 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15537705 | lifeskim:mentions | umls-concept:C0018296 | lld:lifeskim |
| pubmed-article:15537705 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15537705 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:15537705 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:15537705 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15537705 | pubmed:dateCreated | 2004-12-22 | lld:pubmed |
| pubmed-article:15537705 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:15537705 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15537705 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15537705 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15537705 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15537705 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:15537705 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:15537705 | pubmed:author | pubmed-author:ChenShanS | lld:pubmed |
| pubmed-article:15537705 | pubmed:author | pubmed-author:JeddGregoryG | lld:pubmed |
| pubmed-article:15537705 | pubmed:author | pubmed-author:ChenShu HuiSH | lld:pubmed |
| pubmed-article:15537705 | pubmed:author | pubmed-author:LiuFengliF | lld:pubmed |
| pubmed-article:15537705 | pubmed:author | pubmed-author:SegevNavaN | lld:pubmed |
| pubmed-article:15537705 | pubmed:author | pubmed-author:TokarevAndrei... | lld:pubmed |
| pubmed-article:15537705 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15537705 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:15537705 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15537705 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15537705 | pubmed:pagination | 178-92 | lld:pubmed |
