4j2c
From Proteopedia
GARP-SNARE Interaction
Structural highlights
Function[STX6_HUMAN] Involved in intracellular vesicle trafficking. [VPS51_HUMAN] Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi networkl (TGN). The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. VPS51 participates in retrograde transport of acid hydrolase receptors, likely by promoting tethering and SNARE-dependent fusion of endosome-derived carriers to the TGN.[1] Publication Abstract from PubMedThe Golgi-Associated Retrograde Protein (GARP) complex is a tethering factor involved in the fusion of endosome-derived transport vesicles to the trans-Golgi network through interaction with components of the Syntaxin 6/Syntaxin 16/Vti1a/VAMP4 SNARE complex. The mechanisms by which GARP and other tethering factors engage the SNARE fusion machinery are poorly understood. Herein, we report the structural basis for the interaction of the human Ang2 subunit of GARP with the Syntaxin 6 and the closely related Syntaxin 10. The crystal structure of the Syntaxin 6 Habc domain in complex with a peptide from the N terminus of Ang2 shows a binding mode in which a dityrosine motif of Ang2 interacts with a highly conserved groove in Syntaxin 6. Structure-based mutational analyses validate the crystal structure and support the phylogenetic conservation of this interaction. Structural basis for the interaction of the Golgi-Associated Retrograde Protein Complex with the t-SNARE Syntaxin 6.,Abascal-Palacios G, Schindler C, Rojas AL, Bonifacino JS, Hierro A Structure. 2013 Sep 3;21(9):1698-706. doi: 10.1016/j.str.2013.06.025. Epub 2013, Aug 8. PMID:23932592[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
