TY - JOUR
T1 - Interactions within the yeast t-SNARE Sso1p that control SNARE complex assembly
AU - Munson, M.
AU - Chen, X.
AU - Cocina, A. E.
AU - Schultz, S. M.
AU - Hughson, F. M.
N1 - Funding Information:
We thank J. Carey, C. Carr, L. Cavanaugh, E. Grote, R. Miller, S. Miller, P. Novick, B. Reilly, M. Rose, Y. Shi, and G. Waters for gifts of materials and for helpful advice. We are particularly grateful to J. Lerman for guidance in designing mutants and assistance in X-ray data collection. This work was supported by the American Heart Association (M.M.), the Searle Scholars and Beckman Young Investigators programs (F.M.H.), and the N.I.H. (M.M. and F.M.H.).
PY - 2000
Y1 - 2000
N2 - In the eukaryotic secretory and endocytic pathways, transport vesicles shuttle cargo among intracellular organelles and to and from the plasma membrane. Cargo delivery entails fusion of the transport vesicle with its target, a process thought to be mediated by membrane bridging SNARE protein complexes. Temporal and spatial control of intracellular trafficking depends in part on regulating the assembly of these complexes. In vitro, SNARE assembly is inhibited by the closed conformation adopted by the syntaxin family of SNAREs. To visualize this closed conformation directly, the X-ray crystal structure of a yeast syntaxin, Sso1p, has been determined and refined to 2.1 Å resolution. Mutants designed to destabilize the closed conformation exhibit accelerated rates of SNARE assembly. Our results provide insight into the mechanism of SNARE assembly and its intramolecular and intermolecular regulation.
AB - In the eukaryotic secretory and endocytic pathways, transport vesicles shuttle cargo among intracellular organelles and to and from the plasma membrane. Cargo delivery entails fusion of the transport vesicle with its target, a process thought to be mediated by membrane bridging SNARE protein complexes. Temporal and spatial control of intracellular trafficking depends in part on regulating the assembly of these complexes. In vitro, SNARE assembly is inhibited by the closed conformation adopted by the syntaxin family of SNAREs. To visualize this closed conformation directly, the X-ray crystal structure of a yeast syntaxin, Sso1p, has been determined and refined to 2.1 Å resolution. Mutants designed to destabilize the closed conformation exhibit accelerated rates of SNARE assembly. Our results provide insight into the mechanism of SNARE assembly and its intramolecular and intermolecular regulation.
UR - https://www.scopus.com/pages/publications/0033784541
UR - https://www.scopus.com/pages/publications/0033784541#tab=citedBy
U2 - 10.1038/79659
DO - 10.1038/79659
M3 - Article
C2 - 11017200
AN - SCOPUS:0033784541
SN - 1072-8368
VL - 7
SP - 894
EP - 902
JO - Nature Structural Biology
JF - Nature Structural Biology
IS - 10
ER -