Universität zu Köln

Madsen, Louise, Molbaek, Karen, Larsen, Ida B., Nielsen, Sofie V., Poulsen, Esben G., Walmod, Peter S., Hofmann, Kay ORCID: 0000-0002-2289-9083, Seeger, Michael, Chien, Chen-Ying, Chen, Rey-Huei ORCID: 0000-0002-6006-2137, Kriegenburg, Franziska and Hartmann-Petersen, Rasmus ORCID: 0000-0002-4155-7791 (2014). 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 Biol., 15. LONDON: BMC. ISSN 1471-2121

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Abstract

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 complex, known as p97 or VCP in mammals and Cdc48 in yeast. In addition, ASPL interacts in vitro with NSF, another hexameric ATPase complex. ASPL localizes to the ER membrane. The central area in ASPL, containing both a SHP box and a UBX domain, is required for binding to the p97 N domain. Knock down of ASPL does not impair degradation of misfolded secretory proteins via the ERAD pathway. Deletion of UBX4 in yeast causes cycloheximide sensitivity, while ubx4 cdc48-3 double mutations cause proteasome mislocalization. ASPL alleviates these defects, but not the impaired ERAD. Conclusions: In conclusion, ASPL and Ubx4 are homologous proteins with only partially overlapping functions. Both interact with p97/Cdc48, but while Ubx4 is important for ERAD, ASPL appears not to share this function.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Madsen, Louise UNSPECIFIED UNSPECIFIED UNSPECIFIED Molbaek, Karen UNSPECIFIED UNSPECIFIED UNSPECIFIED Larsen, Ida B. UNSPECIFIED UNSPECIFIED UNSPECIFIED Nielsen, Sofie V. UNSPECIFIED UNSPECIFIED UNSPECIFIED Poulsen, Esben G. UNSPECIFIED UNSPECIFIED UNSPECIFIED Walmod, Peter S. UNSPECIFIED UNSPECIFIED UNSPECIFIED Hofmann, Kay UNSPECIFIED orcid.org/0000-0002-2289-9083 UNSPECIFIED Seeger, Michael UNSPECIFIED UNSPECIFIED UNSPECIFIED Chien, Chen-Ying UNSPECIFIED UNSPECIFIED UNSPECIFIED Chen, Rey-Huei UNSPECIFIED orcid.org/0000-0002-6006-2137 UNSPECIFIED Kriegenburg, Franziska UNSPECIFIED UNSPECIFIED UNSPECIFIED Hartmann-Petersen, Rasmus UNSPECIFIED orcid.org/0000-0002-4155-7791 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-433610
DOI:	10.1186/1471-2121-15-31
Journal or Publication Title:	BMC Cell Biol.
Volume:	15
Date:	2014
Publisher:	BMC
Place of Publication:	LONDON
ISSN:	1471-2121
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Biology > Institute for Genetics
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language RETICULUM-ASSOCIATED DEGRADATION; UBIQUITIN-SELECTIVE CHAPERONE; AAA ATPASE CDC48/P97; ENDOPLASMIC-RETICULUM; PROTEIN-DEGRADATION; TRANSCRIPTION FACTOR; DOMAIN PROTEINS; TUG; PATHWAY; CDC48(UFD1/NPL4) Multiple languages Cell Biology Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/43361