Multisubunit tethering complexes (MTCs) interact with soluble SNAREs to couple vesicular tethering with fusion. Conserved Oligomeric Golgi (COG) and Golgi-associated retrograde protein (GARP) MTCs interact with multiple SNAREs on the Golgi membranes. The eight subunits of the COG complex are organized in two structurally and functionally distinct lobes (light and dark blue). The Vps52, Vps53, and Vps54 subunits of GARP (purple) can be assembled into a core complex and localize to the Golgi in the absence of Vps51. The Vps51 subunit (pink) interacts with the N-terminal regulatory Habc domain of Syntaxin (Stx)6 (Tlg1p in yeast). The yeast DSL1 complex according to its crystal structure. DSL1 interacts with the t-SNAREs Sec20 and Use1 via its Tip20 and Sec39 subunits and induces t-SNARE gathering on the endoplasmic reticulum (ER) membrane. The Dsl1p subunit interacts with subunits of the COP-I coat and tethers COP-I vesicles to the ER membranes
