Reference: Boban M, et al. (2015) Atypical ubiquitylation in yeast targets lysine-less Asi2 for proteasomal degradation. J Biol Chem 290(4):2489-95

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Abstract


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.

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Journal Article | Research Support, Non-U.S. Gov't
Authors
Boban M, Ljungdahl PO, Foisner R
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