PMID- 10336434
OWN - NLM
STAT- MEDLINE
DCOM- 19990629
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 22
DP  - 1999 May 28
TI  - Mixed and non-cognate SNARE complexes. Characterization of assembly and
      biophysical properties.
PG  - 15440-6
AB  - Assembly of soluble N-ethylmaleimide-sensitive fusion attachment protein receptor
      (SNARE) proteins between two opposing membranes is thought to be the key event
      that initiates membrane fusion. Many new SNARE proteins have recently been
      localized to distinct intracellular compartments, supporting the view that sets
      of specific SNAREs are specialized for distinct trafficking steps. We have now
      investigated whether other SNAREs can form complexes with components of the
      synaptic SNARE complex including synaptobrevin/VAMP 2, SNAP-25, and syntaxin 1.
      When the Q-SNAREs syntaxin 2, 3, and 4, and the R-SNARE endobrevin/VAMP 8 were
      used in various combinations, heat-resistant complexes were formed. Limited
      proteolysis revealed that these complexes contained a protease-resistant core
      similar to that of the synaptic complex. All complexes were disassembled by the
      ATPase N-ethylmaleimide-sensitive fusion protein and its cofactor alpha-SNAP.
      Circular dichroism spectroscopy showed that major conformational changes occur
      during assembly, which are associated with induction of structure from
      unstructured monomers. Furthermore, no preference for synaptobrevin was observed 
      during the assembly of the synaptic complex when endobrevin/VAMP 8 was present in
      equal concentrations. We conclude that cognate and non-cognate SNARE complexes
      are very similar with respect to biophysical properties, assembly, and
      disassembly, suggesting that specificity of membrane fusion in intracellular
      membrane traffic is not due to intrinsic specificity of SNARE pairing.
FAU - Fasshauer, D
AU  - Fasshauer D
AD  - Department of Neurobiology, Max Planck Institute for Biophysical Chemistry,
      D-37077 Gottingen, Germany.
FAU - Antonin, W
AU  - Antonin W
FAU - Margittai, M
AU  - Margittai M
FAU - Pabst, S
AU  - Pabst S
FAU - Jahn, R
AU  - Jahn R
LA  - eng
SI  - GENBANK/AF132812
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Carrier Proteins)
RN  - 0 (Detergents)
RN  - 0 (Membrane Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Qa-SNARE Proteins)
RN  - 0 (R-SNARE Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (SNARE Proteins)
RN  - 0 (Snap25 protein, rat)
RN  - 0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins)
RN  - 0 (Stx1a protein, rat)
RN  - 0 (Synaptosomal-Associated Protein 25)
RN  - 0 (Syntaxin 1)
RN  - 0 (Vamp8 protein, rat)
RN  - 0 (Vesicular Transport Proteins)
RN  - EC 3.4.21.64 (Endopeptidase K)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Carrier Proteins/metabolism
MH  - Cloning, Molecular
MH  - Detergents
MH  - Endopeptidase K/metabolism
MH  - Membrane Fusion
MH  - Membrane Proteins/chemistry/genetics/*metabolism
MH  - Molecular Sequence Data
MH  - Nerve Tissue Proteins/chemistry/*metabolism
MH  - Protein Structure, Secondary
MH  - Qa-SNARE Proteins
MH  - R-SNARE Proteins
MH  - Rats
MH  - Recombinant Proteins/metabolism
MH  - SNARE Proteins
MH  - Sequence Alignment
MH  - Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
MH  - Synaptosomal-Associated Protein 25
MH  - Syntaxin 1
MH  - *Vesicular Transport Proteins
EDAT- 1999/05/21 00:00
MHDA- 1999/05/21 00:01
CRDT- 1999/05/21 00:00
PHST- 1999/05/21 00:00 [pubmed]
PHST- 1999/05/21 00:01 [medline]
PHST- 1999/05/21 00:00 [entrez]
AID - 10.1074/jbc.274.22.15440 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 May 28;274(22):15440-6. doi: 10.1074/jbc.274.22.15440.