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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 J+Mol+Biol
2016 ; 428
(9 Pt B
): 1912-26
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Recent Advances in Deciphering the Structure and Molecular Mechanism of the AAA+
ATPase N-Ethylmaleimide-Sensitive Factor (NSF)
#MMPMID26546278
Zhao M
; Brunger AT
J Mol Biol
2016[May]; 428
(9 Pt B
): 1912-26
PMID26546278
show ga
N-ethylmaleimide-sensitive factor (NSF), first discovered in 1988, is a key
factor for eukaryotic trafficking, including protein and hormone secretion and
neurotransmitter release. It is a member of the AAA+ family (ATPases associated
with diverse cellular activities). NSF disassembles soluble
N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes
in conjunction with soluble N-ethylmaleimide-sensitive factor attachment protein
(SNAP). Structural studies of NSF and its complex with SNAREs and SNAPs (known as
20S supercomplex) started about 20years ago. Crystal structures of individual N
and D2 domains of NSF and low-resolution electron microscopy structures of
full-length NSF and 20S supercomplex have been reported over the years.
Nevertheless, the molecular architecture of the 20S supercomplex and the
molecular mechanism of NSF-mediated SNARE complex disassembly remained unclear
until recently. Here we review recent atomic-resolution or near-atomic resolution
structures of NSF and of the 20S supercomplex, as well as recent insights into
the molecular mechanism and energy requirements of NSF. We also compare NSF with
other known AAA+ family members.