Journal
EMBO REPORTS
Volume 8, Issue 12, Pages 1176-1182Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.embor.7401105
Keywords
ERAD; SM proteins; SNARE; ubiquitin; Ufe1
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Endoplasmic reticulum (ER)- associated degradation (ERAD) is a specialized activity of the ubiquitin - proteasome system that is involved in clearing the ER of aberrant proteins and regulating the levels of specific ER-resident proteins. Here we show that the yeast ER-SNARE Ufe1, a syntaxin (Qa-SNARE) involved in ER membrane fusion and retrograde transport from the Golgi to the ER, is prone to degradation by an ERAD-like mechanism. Notably, Ufe1 is protected against degradation through binding to Sly1, a known SNARE regulator of the Sec1-Munc18 (SM) protein family. This mechanism is specific for Ufe1, as the stability of another Sly1 partner, the Golgi Qa-SNARE Sed5, is not influenced by Sly1 interaction. Thus, our findings identify Sly1 as a discriminating regulator of SNARE levels and indicate that Sly1-controlled ERAD might regulate the balance between different Qa-SNARE proteins.
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