Structural insights into the molecular mechanism of calcium-dependent vesicle-membrane fusion
1The Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305, USA. axel.brunger@stanford.edu
Abstract:
The fusion of vesicles with target membranes is controlled by a complex network of protein-protein and protein-lipid interactions. Recently determined structures of the SNARE complex, synaptotagmin III, nSec1, domains of the NSF chaperone and its adaptor (SNAP), and Rab3 and some of its effectors provide the framework for developing molecular models of vesicle fusion and for designing experiments to test these models. Ultimately, knowledge of the structures of higher-order complexes and their dynamic behavior will be required to obtain a full understanding of the vesicle fusion protein machinery.
Related Concept Videos
Overview of Secretory Vesicles
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Fusion of Secretory Vesicles with the Plasma Membrane
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
Pinching-off of Coated Vesicles
SNAREs and Membrane Fusion
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
Vesicular Tubular Clusters
With the help of motor proteins such...
Clathrin Coated Vesicles


