PMID- 10559959
OWN - NLM
STAT- MEDLINE
DCOM- 20000908
LR  - 20131121
IS  - 1465-7392 (Print)
IS  - 1465-7392 (Linking)
VI  - 1
IP  - 6
DP  - 1999 Oct
TI  - An NSF function distinct from ATPase-dependent SNARE disassembly is essential for
      Golgi membrane fusion.
PG  - 335-40
AB  - The precise biochemical role of N-ethylmaleimide-sensitive factor (NSF) in
      membrane fusion mediated by SNARE proteins is unclear. To provide further insight
      into the function of NSF, we have introduced a mutation into mammalian NSF that, 
      in Drosophila dNSF-1, leads to temperature-sensitive neuroparalysis. This
      mutation is like the comatose mutation and renders the mammalian NSF temperature 
      sensitive for fusion of postmitotic Golgi vesicles and tubules into intact
      cisternae. Unexpectedly, at the temperature that is permissive for membrane
      fusion, this mutant NSF binds to, but cannot disassemble, SNARE complexes and
      exhibits almost no ATPase activity. A well-charaterized NSF mutant containing an 
      inactivating point mutation in the catalytic site of its ATPase domain is equally
      active in the Golgi-reassembly assay. These data indicate that the need for NSF
      during postmitotic Golgi membrane fusion may be distinct from its
      ATPase-dependent ability to break up SNARE pairs.
FAU - Muller, J M
AU  - Muller JM
AD  - Cell Biology Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, 
      London WC2A 3PX, UK.
FAU - Rabouille, C
AU  - Rabouille C
FAU - Newman, R
AU  - Newman R
FAU - Shorter, J
AU  - Shorter J
FAU - Freemont, P
AU  - Freemont P
FAU - Schiavo, G
AU  - Schiavo G
FAU - Warren, G
AU  - Warren G
FAU - Shima, D T
AU  - Shima DT
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Nat Cell Biol
JT  - Nature cell biology
JID - 100890575
RN  - 0 (Carrier Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Nucleotides)
RN  - 0 (SNARE Proteins)
RN  - 0 (Vesicular Transport Proteins)
RN  - 0 (comt protein, Drosophila)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
RN  - EC 3.6.4.6 (N-Ethylmaleimide-Sensitive Proteins)
RN  - O3C74ACM9V (Ethylmaleimide)
SB  - IM
CIN - Nat Cell Biol. 1999 Oct;1(6):E141-3. PMID: 10559970
MH  - Adenosine Triphosphatases/metabolism/*physiology
MH  - Animals
MH  - CHO Cells
MH  - Carrier Proteins/genetics/metabolism/*physiology
MH  - Cricetinae
MH  - Drosophila
MH  - Ethylmaleimide/*metabolism/pharmacology
MH  - Golgi Apparatus/metabolism/*physiology
MH  - Intracellular Membranes/*physiology
MH  - Membrane Fusion/*physiology
MH  - Membrane Proteins/*metabolism
MH  - Mitosis
MH  - Mutagenesis, Site-Directed
MH  - N-Ethylmaleimide-Sensitive Proteins
MH  - Nucleotides
MH  - Protein Conformation
MH  - SNARE Proteins
MH  - Temperature
MH  - *Vesicular Transport Proteins
EDAT- 1999/11/24 09:00
MHDA- 2000/09/19 11:01
CRDT- 1999/11/24 09:00
PHST- 1999/11/24 09:00 [pubmed]
PHST- 2000/09/19 11:01 [medline]
PHST- 1999/11/24 09:00 [entrez]
AID - 10.1038/14025 [doi]
PST - ppublish
SO  - Nat Cell Biol. 1999 Oct;1(6):335-40. doi: 10.1038/14025.