Article
Human ASPL/TUG interacts with p97 and complements the proteasome mislocalization of a yeast ubx4 mutant, but not the ER-associated degradation defect.
BMC cell biology - 31 Jul 2014
Madsen Louise, Molbæk Karen, Larsen Ida B, Nielsen Sofie V, Poulsen Esben G, Walmod Peter S, Hofmann Kay, Seeger Michael, Chien Chen-Ying, Chen Rey-Huei, Kriegenburg Franziska, Hartmann-Petersen Rasmus
Abstract excerpt
BACKGROUND: In mammalian cells, ASPL is involved in insulin-stimulated redistribution of the glucose transporter GLUT4 and assembly of the Golgi apparatus. Its putative yeast orthologue, Ubx4, is important for proteasome localization, endoplasmic reticulum-associated protein degradation (ERAD), and UV-induced degradation of RNA polymerase. RESULTS: Here, we show that ASPL is a cofactor of the hexameric ATPase...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.