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http://purl.uniprot.org/citations/23452853http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23452853http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23452853http://www.w3.org/2000/01/rdf-schema#comment"Endosomal protein trafficking is an essential cellular process that is deregulated in several diseases and targeted by pathogens. Here, we describe a role for ubiquitination in this process. We find that the E3 RING ubiquitin ligase, MAGE-L2-TRIM27, localizes to endosomes through interactions with the retromer complex. Knockdown of MAGE-L2-TRIM27 or the Ube2O E2 ubiquitin-conjugating enzyme significantly impaired retromer-mediated transport. We further demonstrate that MAGE-L2-TRIM27 ubiquitin ligase activity is required for nucleation of endosomal F-actin by the WASH regulatory complex, a known regulator of retromer-mediated transport. Mechanistic studies showed that MAGE-L2-TRIM27 facilitates K63-linked ubiquitination of WASH K220. Significantly, disruption of WASH ubiquitination impaired endosomal F-actin nucleation and retromer-dependent transport. These findings provide a cellular and molecular function for MAGE-L2-TRIM27 in retrograde transport, including an unappreciated role of K63-linked ubiquitination and identification of an activating signal of the WASH regulatory complex."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2013.01.051"xsd:string
http://purl.uniprot.org/citations/23452853http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2013.01.051"xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Chen Z.J."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Chen Z.J."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Xu M."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Xu M."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Doyle J.M."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Doyle J.M."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Billadeau D.D."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Billadeau D.D."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Gomez T.S."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Gomez T.S."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Rosen M.K."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Rosen M.K."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Jia D."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Jia D."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Ramanathan S."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Ramanathan S."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Potts P.R."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Potts P.R."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Hao Y.H."xsd:string
http://purl.uniprot.org/citations/23452853http://purl.uniprot.org/core/author"Hao Y.H."xsd:string