Article
The Dsl1 tethering complex actively participates in soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (SNARE) complex assembly at the endoplasmic reticulum in Saccharomyces cerevisiae.
The Journal of biological chemistry - 15 Jul 2011
Diefenbacher Melanie, Thorsteinsdottir Holmfridur, Spang Anne
Abstract excerpt
Intracellular transport is largely dependent on vesicles that bud off from one compartment and fuse with the target compartment. The first contact of an incoming vesicle with the target membrane is mediated by tethering factors. The tethering factor responsible for recruiting Golgi-derived vesicles to the ER is the Dsl1 tethering complex, which is comprised of the essential proteins Dsl1p, Dsl3p, and Tip20p. We...
Topics
- Endoplasmic Reticulum
- Golgi Apparatus
- Multiprotein Complexes
- Mutation
- Protein Structure, Tertiary
- SNARE Proteins
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
- Vesicular Transport Proteins