Naslov
Atypical ubiquitylation in yeast targets lysine-less Asi2 for proteasomal degradation
(Atypical Ubiquitylation in Yeast Targets Lysine-less Asi2 for Proteasomal Degradation)

Autori
Boban, Mirta ; Ljungdahl, Per O. ; Foisner, Roland

Izvornik
The Journal of biological chemistry (0021-9258) 290 (2014), 4; 2489-2495

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
nuclear envelope, ubiquitin

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Biologija

POVEZANOST RADA