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SM‐protein‐controlled ER‐associated degradation discriminates between different SNAREs
Author(s) -
Braun Sigurd,
Jentsch Stefan
Publication year - 2007
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7401105
Subject(s) - endoplasmic reticulum associated protein degradation , endoplasmic reticulum , microbiology and biotechnology , golgi apparatus , syntaxin , chemistry , protein degradation , vesicular transport proteins , ubiquitin , biology , membrane protein , biochemistry , unfolded protein response , intracellular , membrane , endosome , vacuolar protein sorting , gene
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.