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

Authors: Laufman, O  Kedan, A  Hong, W  Lev, S 
Citation: Laufman O, etal., EMBO J. 2009 Jul 22;28(14):2006-17. doi: 10.1038/emboj.2009.168. Epub 2009 Jun 18.
Pubmed: (View Article at PubMed) PMID:19536132
DOI: Full-text: DOI:10.1038/emboj.2009.168

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.


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RGD Object Information
RGD ID: 8554815
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.