Atypical ubiquitylation in yeast targets lysine-less Asi2 for proteasomal degradation.

Proteins are typically targeted for proteasomal degradation by the attachment of a polyubiquitin chain to ϵ-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. © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

Citation

Mirta Boban, Per O Ljungdahl, Roland Foisner. Atypical ubiquitylation in yeast targets lysine-less Asi2 for proteasomal degradation. The Journal of biological chemistry. 2015 Jan 23;290(4):2489-95

Mesh Tags

Substances

PMID: 25492870

search → result