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Human ASPL/TUG interacts with p97 and complements the proteasome mislocalization of a yeast ubx4 mutant, but not the ER-associated degradation defect

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...

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Main Authors:	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
פורמט:	Artigo
שפה:	Inglês
יצא לאור:	BioMed Central 2014
נושאים:	Research Article
גישה מקוונת:	https://ncbi.nlm.nih.gov/pmc/articles/PMC4124494/ https://ncbi.nlm.nih.gov/pubmed/25078495 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/1471-2121-15-31
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Human ASPL/TUG interacts with p97 and complements the proteasome mislocalization of a yeast ubx4 mutant, but not the ER-associated degradation defect

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