| http://purl.uniprot.org/citations/25561732 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25561732 | http://www.w3.org/2000/01/rdf-schema#comment | "Rho GTPases are molecular switches that modulate a variety of cellular processes, most notably those involving actin dynamics. We have previously shown that yeast vacuolar membrane fusion requires re-organization of actin filaments mediated by two Rho GTPases, Rho1p and Cdc42p. Cdc42p initiates actin polymerization to facilitate membrane tethering; Rho1p has a role in the late stages of vacuolar fusion, but its mode of action is unknown. Here, we identified eEF1A as a vacuolar Rho1p-interacting protein. eEF1A (encoded by the TEF1 and TEF2 genes in yeast) is an aminoacyl-tRNA transferase needed during protein translation. eEF1A also has a second function that is independent of translation; it binds and organizes actin filaments into ordered cable structures. Here, we report that eEF1A interacts with Rho1p via a C-terminal subdomain. This interaction occurs predominantly when both proteins are in the GDP-bound state. Therefore, eEF1A is an atypical downstream effector of Rho1p. eEF1A does not promote vacuolar fusion; however, overexpression of the Rho1p-interacting subdomain affects vacuolar morphology. Vacuoles were destabilized and prone to leakage when treated with the eEF1A inhibitor narciclasine. We propose a model whereby eEF1A binds to Rho1p-GDP on the vacuolar membrane; it is released upon Rho1p activation and then bundles actin filaments to stabilize fused vacuoles. Therefore, the Rho1p-eEF1A complex acts to spatially localize a pool of eEF1A to vacuoles where it can readily organize F-actin."xsd:string |
| http://purl.uniprot.org/citations/25561732 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m114.630764"xsd:string |
| http://purl.uniprot.org/citations/25561732 | http://purl.uniprot.org/core/author | "Yang Y."xsd:string |
| http://purl.uniprot.org/citations/25561732 | http://purl.uniprot.org/core/author | "Logan M.R."xsd:string |
| http://purl.uniprot.org/citations/25561732 | http://purl.uniprot.org/core/author | "Eitzen G."xsd:string |
| http://purl.uniprot.org/citations/25561732 | http://purl.uniprot.org/core/author | "Bodman J.A.R."xsd:string |
| http://purl.uniprot.org/citations/25561732 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
| http://purl.uniprot.org/citations/25561732 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/25561732 | http://purl.uniprot.org/core/pages | "4705-4716"xsd:string |
| http://purl.uniprot.org/citations/25561732 | http://purl.uniprot.org/core/title | "Yeast translation elongation factor-1A binds vacuole-localized Rho1p to facilitate membrane integrity through F-actin remodeling."xsd:string |
| http://purl.uniprot.org/citations/25561732 | http://purl.uniprot.org/core/volume | "290"xsd:string |
| http://purl.uniprot.org/citations/25561732 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25561732 |
| http://purl.uniprot.org/citations/25561732 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/25561732 |
| http://purl.uniprot.org/uniprot/P02994#attribution-78E3412DFF56A979BFA546DFB1854811 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/25561732 |
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| http://purl.uniprot.org/uniprot/#_P02994-mappedCitation-25561732 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25561732 |
| http://purl.uniprot.org/uniprot/#_P06780-mappedCitation-25561732 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/25561732 |
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| http://purl.uniprot.org/uniprot/P02994 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/25561732 |