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Atypical Ubiquitylation in Yeast Targets Lysine-less Asi2 for Proteasomal Degradation
Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
2015 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 290, no 4, 2489-2495 p.Article in journal (Refereed) Published
Abstract [en]

Proteins are typically targeted for proteasomal degradation by the attachment of a polyubiquitin chain to epsilon-amino groups of lysine residues. Non-lysine ubiquitylation of proteasomal substrates has been considered an atypical and rare event limited to complex eukaryotes. Here we report that a fully functional lysine-less mutant of an inner nuclear membrane protein in yeast, Asi2, is polyubiquitylated and targeted for proteasomal degradation. Efficient degradation of lysine-free Asi2 requires E3-ligase Doa10 and E2 enzymes Ubc6 and Ubc7, components of the endoplasmic reticulum-associated degradation pathway. Together, our data suggest that non-lysine ubiquitylation may be more prevalent than currently considered.

Place, publisher, year, edition, pages
2015. Vol. 290, no 4, 2489-2495 p.
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-115300DOI: 10.1074/jbc.M114.600593ISI: 000348588000050PubMedID: 25492870OAI: oai:DiVA.org:su-115300DiVA: diva2:799913
Note

AuthorCount:3;

Available from: 2015-03-31 Created: 2015-03-18 Last updated: 2017-12-04Bibliographically approved

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