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Cdc48 and Ubx1 participate in a pathway associated with the inner nuclear membrane that governs Asi1 degradation
Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
Number of Authors: 4
2016 (English)In: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 129, no 20, 3770-3780 p.Article in journal (Refereed) Published
Abstract [en]

The nuclear envelope is a barrier comprising outer and inner membranes that separate the cytoplasm from the nucleoplasm. The two membranes have different physical characteristics and protein compositions. The processes governing the stability of inner nuclear membrane (INM) proteins are not well characterized. In Saccharomyces cerevisiae, the INM Asi1-Asi3 complex, principally composed of integral membrane proteins Asi1 and Asi3, is an E3 ubiquitin ligase. In addition to its well-documented function in endoplasmic reticulum (ER)-associated degradation, the Doa10 E3 ubiquitin ligase complex partially localizes to the INM. The Asi1-Asi3 and Doa10 complexes define independent INM-associated degradation (INMAD) pathways that target discrete sets of nuclear substrates for proteasomal degradation. Here, we report that Asi1 is rapidly turned over (t(1/2)<= 30 min). Its turnover depends on ubiquitin-mediated degradation by nucleus-localized proteasomes, exhibiting a clear requirement for the E2 ubiquitin-conjugating enzyme Ubc7, Cue1 and the AAA ATPase Cdc48 and co-factor Ubx1. Asi1 turnover occurs largely independently of the Asi1-Asi3 or Doa10 complexes, indicating that it is subject to quality control at the INM in a manner distinct from that of the characterized INMAD pathways.

Place, publisher, year, edition, pages
2016. Vol. 129, no 20, 3770-3780 p.
Keyword [en]
Nuclear envelope, Ubiquitin, Proteasome, Inner nuclear-membrane-associated degradation, INMAD, Membrane dislocation, Saccharomyces cerevisiae
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-137518DOI: 10.1242/jcs.189332ISI: 000389595200008PubMedID: 27566164OAI: oai:DiVA.org:su-137518DiVA: diva2:1066414
Available from: 2017-01-18 Created: 2017-01-09 Last updated: 2017-01-18Bibliographically approved

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Pantazopoulou, MarinaLjungdahl, Per O.
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