title: The DSL1 complex: the smallest but not the least CATCHR.
abstract: 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 DSL1 complex is the simplest tethering complex of the complexes associated with tethering containing helical rods (CATCHR) family. CATCHR tethering complexes play a role at compartments along the exocytic and endocytic pathways. In this review, different functions of the DSL1 complex are discussed, some open questions with the seemingly straightforward picture are pointed out and alternative functions of the DSL1 complex members are mentioned.
authors.affiliation: Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. anne.spang@unibas.ch
authors.forename: Anne
authors.initials: A
authors.lastname: Spang
mesh_terms: D000818:Animals; D022181:COP-Coated Vesicles / Q000502:physiology*; D004705:Endocytosis; D005089:Exocytosis; D006801:Humans; D008561:Membrane Fusion; D050765:Qa-SNARE Proteins / Q000502:physiology*; D015003:Yeasts
chemical_list: D050765:Qa-SNARE Proteins