The BioGRID | PUBLICATION VIEW

	EMBO Rep. Dec (2007); 8(12):1176-82
SM-protein-controlled ER-associated degradation discriminates between different SNAREs-
Braun S, Jentsch S
Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried, Munich D-82152, Germany-
Abstract: 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-
[PUBMED: 18007658]