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NSF and p97/VCP: similar at first, different at last
Author(s) -
Brunger Axel T.,
DeLaBarre Byron
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01107-4
Subject(s) - vesicle , aaa proteins , lipid bilayer fusion , microbiology and biotechnology , snare complex , chemistry , vesicle fusion , biology , atpase , biophysics , membrane , biochemistry , enzyme , synaptic vesicle
N ‐Ethylmaleimide sensitive factor (NSF) and p97/valosin‐containing protein (VCP) are distantly related members of the ATPases associated with a variety of cellular activities (AAA) family of proteins. While both proteins have been implied in cellular morphology changes involving membrane compartments or vesicles, more recent evidence seems to imply that NSF is primarily involved in the soluble NSF attachment receptor (SNARE)‐mediated vesicle fusion by disassembling the SNARE complex whereas p97/VCP is primarily involved in the extraction of membrane proteins. These functional differences are now corroborated by major structural differences based on recent crystallographic and cryo‐electron microscopy studies. This review discusses these recent findings.