Structural insights into the molecular mechanism of calcium-dependent vesicle-membrane fusion.

A T Brunger
Author Information
  1. A T Brunger: The 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.

MeSH Term

Animals
Calcium
Calcium-Binding Proteins
Carrier Proteins
Membrane Fusion
Membrane Glycoproteins
Membrane Proteins
N-Ethylmaleimide-Sensitive Proteins
Nerve Tissue Proteins
SNARE Proteins
Saccharomyces cerevisiae Proteins
Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
Synaptotagmins
Transport Vesicles
Vesicular Transport Proteins
rab3A GTP-Binding Protein

Chemicals

Calcium-Binding Proteins
Carrier Proteins
Membrane Glycoproteins
Membrane Proteins
Nerve Tissue Proteins
SEC17 protein, S cerevisiae
SNARE Proteins
Saccharomyces cerevisiae Proteins
Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
Vesicular Transport Proteins
Synaptotagmins
N-Ethylmaleimide-Sensitive Proteins
rab3A GTP-Binding Protein
Calcium

Word Cloud

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