title: At the junction of SNARE and SM protein function.
abstract: Sec1/Munc18 (SM) proteins bind to and function with soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) at each vesicle fusion site in the cell. The purpose for these interactions is becoming clearer, as what had been interpreted as functional divergence between SM proteins acting at different vesicle trafficking steps, or in specialized cells, is giving way to more recent evidence for common functions among all SM proteins. What is emerging is a picture of SM proteins acting not merely as SNARE regulators, but also as central components of the membrane fusion apparatus. The available data suggest sequential models that describe how the soluble SM protein might first regulate SNARE complex assembly and then cooperate with SNAREs to stimulate membrane fusion.
authors.affiliation: Department of Biochemistry and Biophysics, Texas A&M University, 300 Olsen Blvd., College Station, TX 77843-2128, USA. chave@tamu.edu
authors.forename: Chavela M
authors.initials: CM
authors.lastname: Carr
authors.forename: Josep
authors.initials: J
authors.lastname: Rizo
mesh_terms: D000818:Animals; D006801:Humans; D008561:Membrane Fusion; D008954:Models, Biological; D051938:Munc18 Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D050765:Qa-SNARE Proteins / Q000737:chemistry / Q000378:metabolism; D050600:SNARE Proteins / Q000378:metabolism*
chemical_list: D051938:Munc18 Proteins; D050765:Qa-SNARE Proteins; D050600:SNARE Proteins
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