Fusion of Golgi-derived COP (coat protein)-I vesicles with the endoplasmic reticulum (ER) is
initiated by specific tethering complexes: the Dsl1 (depends on SLY1-20) complex in yeast …

Multisubunit tethering complexes are essential for intracellular trafficking and have been
proposed to mediate the initial interaction between vesicles and the membranes with which …

The yeast Dsl1p vesicle tethering complex, comprising the three subunits Dsl1p, Dsl3p, and
Tip20p, is stably associated with three endoplasmic reticulum-localized Q-SNAREs and is …

The DSL1 complex is a conserved tethering complex at the endoplasmic reticulum that
recognizes Golgi‐derived COPI vesicles and hands them over to the fusion machinery. The …

Multisubunit-tethering complexes (MTCs) are large (250 to> 750 kDa), conserved
macromolecular machines that are essential for soluble N-ethylmaleimide–sensitive factor …

Vesicle trafficking requires membrane fusion, mediated by SNARE proteins, and upstream
events that probably include" tethering," an initial long-range attachment between a vesicle …

Membrane fusion in all eukaryotic cells is regulated by the formation of specific SNARE
(soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complexes. The …

The essential Golgi protein Sly1 is a member of the Sec1/mammalian Unc-18 (SM) family of
SNARE chaperones. Sly1 was originally identified through remarkable gain-of-function …

Retrograde vesicular transport from the Golgi to the ER requires the Dsl1 tethering complex,
which consists of the three subunits Dsl1, Dsl3, and Tip20. It forms a stable complex with the …

Cytosolic Sec1/munc18‐like proteins (SM proteins) are recruited to membrane fusion sites
by interaction with syntaxin‐type SNARE proteins, constituting indispensable positive …