| http://purl.uniprot.org/citations/21686101 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21686101 | http://www.w3.org/2000/01/rdf-schema#comment | "Ypt/Rab GTPases are conserved molecular switches that regulate the different steps of intracellular trafficking pathways. In yeast, the Ypt31/32 GTPases are required for exit from the trans-Golgi and for recycling from the plasma membrane (PM), through early endosomes, to the Golgi. We have previously shown that the recycling function of Ypt31/32 is mediated by an effector called Rcy1. Specifically, both Ypt31/32 and Rcy1 are required for recycling the vSNARE Snc1. Rcy1 contains an F-box domain shared by proteins that act in substrate recognition of ubiquitin ligases. Here, we show that both Ypt31/32 and Rcy1 are important for Snc1 ubiquitination and that such ubiquitination plays a role in Snc1 recycling. Direct interaction between Rcy1 and Snc1 was demonstrated using two independent approaches. In vitro interaction was observed using co-precipitation of recombinant proteins, whereas interaction in yeast cells was observed using bimolecular fluorescence complementation. Ubiquitination of Snc1 in vivo at the K63 position was previously shown in a proteomic study. We show that the Snc1-K63R mutant protein is less ubquitinated than wild-type Snc1 and is defective in endosome-to-Golgi transport. Additionally, wild-type Snc1 is ubiquitinated to a lesser extent in ypt31/32ts and rcy1Δ mutant cells and Snc1 recycling is also blocked in endosomes in these mutants. Therefore, ubiquitination plays a role in the recycling of Snc1 from the PM to the Golgi, and Ypt31/32 and Rcy1 regulate this ubiquitination. Together, these results suggest a new role for ubiquitination in cargo recycling. Moreover, we propose that Ypt/Rabs integrate intra-cellular trafficking with ubiquitination."xsd:string |
| http://purl.uniprot.org/citations/21686101 | http://purl.org/dc/terms/identifier | "doi:10.4161/cl.1.1.14695"xsd:string |
| http://purl.uniprot.org/citations/21686101 | http://purl.uniprot.org/core/author | "Shah A.H."xsd:string |
| http://purl.uniprot.org/citations/21686101 | http://purl.uniprot.org/core/author | "Segev N."xsd:string |
| http://purl.uniprot.org/citations/21686101 | http://purl.uniprot.org/core/author | "Chen S.H."xsd:string |
| http://purl.uniprot.org/citations/21686101 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21686101 | http://purl.uniprot.org/core/name | "Cell Logist"xsd:string |
| http://purl.uniprot.org/citations/21686101 | http://purl.uniprot.org/core/pages | "21-31"xsd:string |
| http://purl.uniprot.org/citations/21686101 | http://purl.uniprot.org/core/title | "Ypt31/32 GTPases and their F-Box effector Rcy1 regulate ubiquitination of recycling proteins."xsd:string |
| http://purl.uniprot.org/citations/21686101 | http://purl.uniprot.org/core/volume | "1"xsd:string |
| http://purl.uniprot.org/citations/21686101 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21686101 |
| http://purl.uniprot.org/citations/21686101 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21686101 |
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| http://purl.uniprot.org/uniprot/#_P38555-mappedCitation-21686101 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21686101 |
| http://purl.uniprot.org/uniprot/#_P39531-mappedCitation-21686101 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21686101 |
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| http://purl.uniprot.org/uniprot/P39531 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/21686101 |
| http://purl.uniprot.org/uniprot/P31109 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/21686101 |
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