Atypical Ubiquitylation in Yeast Targets Lysine-less Asi2 for Proteasomal Degradation (CROSBI ID 264659)
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Podaci o odgovornosti
Boban, Mirta ; Ljungdahl, Per O. ; Foisner, Roland
engleski
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.
nuclear envelope, ubiquitin
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Podaci o izdanju
290 (4)
2014.
2489-2495
objavljeno
0021-9258
1083-351X
10.1074/jbc.m114.600593