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RNF41 interacts with the VPS52 subunit of the GARP and EARP complexes

Tijdschriftbijdrage - Tijdschriftartikel

RNF41 (Ring Finger Protein 41) is an E3 ubiquitin ligase involved in the intracellular sorting and function of a diverse set of substrates. Next to BRUCE and Parkin, RNF41 can directly ubiquitinate ErbB3, IL-3, EPO and RARa receptors or downstream signaling molecules such as Myd88, TBK1 and USP8. In this way it can regulate receptor signaling and routing. To further elucidate the molecular mechanism behind the role of RNF41 in intracellular transport we performed an Array MAPPIT (Mammalian Protein-Protein Interaction Trap) screen using an extensive set of proteins derived from the human ORFeome collection. This paper describes the identification of VPS52, a subunit of the GARP (Golgi-Associated Retrograde Protein) and the EARP (Endosome-Associated Recycling Protein) complexes, as a novel interaction partner of RNF41. Through interaction via their coiled coil domains, RNF41 ubiquitinates and relocates VPS52 away from VPS53, a common subunit of the GARP and EARP complexes, towards RNF41 bodies.
Tijdschrift: PLOS ONE
ISSN: 1932-6203
Issue: 5
Volume: 12
Jaar van publicatie:2017
BOF-keylabel:ja
IOF-keylabel:ja
BOF-publication weight:2
CSS-citation score:1
Auteurs:International
Authors from:Government
Toegankelijkheid:Open