Chaperoning SNARE assembly and disassembly.
Intracellular membrane fusion is mediated in most cases by membrane-bridging complexes of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). However, the assembly of such complexes in vitro is inefficient, and their uncatalysed disassembly is undetectably slow. Here, we focus on the cellular machinery that orchestrates assembly and disassembly of SNARE complexes, thereby regulating processes ranging from vesicle trafficking to organelle fusion to neurotransmitter release. Rapid progress is being made on many fronts, including the development of more realistic cell-free reconstitutions, the application of single-molecule biophysics, and the elucidation of X-ray and high-resolution electron microscopy structures of the SNARE assembly and disassembly machineries 'in action'.
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.|Present address: Department of Cellular and Molecular Medicine, School of Medicine, University of California San Diego, La Jolla, California 92093, USA.
Richard W
RW
Baker
Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544, USA.
Frederick M
FM
Hughson
D000818:Animals; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D050600:SNARE Proteins / Q000378:metabolism*
D018832:Molecular Chaperones; D050600:SNARE Proteins