Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing

被引：86

作者：

Laufman, Orly ^{[1
]}

Kedan, Amir ^{[1
]}

Hong, Wanjin ^{[2
]}

Lev, Sima ^{[1
]}

机构：

[1] Weizmann Inst Sci, Dept Mol Cell Biol, IL-76100 Rehovot, Israel

[2] Biopolis, Inst Mol & Cell Biol, Canc & Dev Cell Biol Div, Singapore, Singapore

来源：

EMBO JOURNAL | 2009年 / 28卷 / 14期

关键词：

COG; Golgi; retrograde transport; SM proteins; SNARE pairing; MEDIATED MEMBRANE-FUSION; ENDOPLASMIC-RETICULUM; RETROGRADE TRANSPORT; CONGENITAL DISORDER; TETHERING COMPLEXES; BREFELDIN-A; VESICLE; BINDING; SYNTAXIN; ER;

D O I：

10.1038/emboj.2009.168

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

The crucial roles of Sec1/Munc18 (SM)-like proteins in membrane fusion have been evidenced in genetic and biochemical studies. SM proteins interact directly with SNAREs and contribute to SNARE pairing by a yet unclear mechanism. Here, we show that the SM protein, Sly1, interacts directly with the conserved oligomeric Golgi (COG) tethering complex. The Sly1-COG interaction is mediated by the Cog4 subunit, which also interacts with Syntaxin 5 through a different binding site. We provide evidence that disruption of Cog4-Sly1 interaction impairs pairing of SNAREs involved in intra-Golgi transport thereby markedly attenuating Golgi-to-ER retrograde transport. These results highlight the mechanism by which SM proteins link tethering to SNAREpin assembly. The EMBO Journal (2009) 28, 2006-2017. doi: 10.1038/emboj.2009.168; Published online 18 June 2009

引用

页码：2006 / 2017

页数：12

共 66 条

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