PMID- 10051443
OWN - NLM
STAT- MEDLINE
DCOM- 19990504
LR  - 20181113
IS  - 0264-6021 (Print)
IS  - 0264-6021 (Linking)
VI  - 338 ( Pt 3)
DP  - 1999 Mar 15
TI  - SNAP-23 participates in SNARE complex assembly in rat adipose cells.
PG  - 709-15
AB  - SNARE proteins are required for vesicle docking and fusion in eukaryotic cells in
      processes as diverse as homotypic membrane fusion and synaptic vesicle exocytosis
      [SNARE stands for SNAP receptor, where SNAP is soluble NSF attachment protein].
      The SNARE proteins syntaxin 4 and vesicle-associated membrane protein (VAMP) 2/3 
      also participate in the insulin-stimulated translocation of GLUT4 from
      intracellular vesicles to the plasma membrane in adipose cells. We now report the
      molecular cloning and characterization of rat SNAP-23, a ubiquitously expressed
      homologue of the essential neuronal SNARE protein SNAP-25
      (synaptosomal-associated protein of 25 kDa). Rat SNAP-23 is 86% and 98% identical
      respectively to human and mouse SNAP-23. Southern blot analysis reveals that the 
      rat, mouse and human SNAP-23 genes encode species-specific isoforms of the same
      protein. Co-immunoprecipitation of syntaxin 4 and SNAP-23 shows association of
      these two proteins in rat adipose cell plasma membranes, and insulin stimulation 
      does not alter the SNAP-23/syntaxin 4 complex. In addition, we demonstrate for
      the first time the participation of SNAP-23, along with syntaxin 4 and VAMP2/3,
      in the formation of 20S SNARE complexes prepared using rat adipose cell membranes
      and recombinant alpha-SNAP and NSF proteins. The stoichiometry of the SNARE
      complexes formed is essentially identical using membranes from either
      unstimulated or insulin-stimulated adipose cells. These data demonstrate that rat
      SNAP-23 associates with syntaxin 4 before insulin stimulation and is present in
      the SNARE complexes known to mediate the translocation of GLUT4 from
      intracellular vesicles to the plasma membrane of rat adipose cells.
FAU - St-Denis, J F
AU  - St-Denis JF
AD  - Experimental Diabetes, Metabolism, and Nutrition Section, Diabetes Branch,
      National Institute of Diabetes and Digestive and Kidney Diseases, National
      Institutes of Health, Bethesda, MD 20892, USA.
FAU - Cabaniols, J P
AU  - Cabaniols JP
FAU - Cushman, S W
AU  - Cushman SW
FAU - Roche, P A
AU  - Roche PA
LA  - eng
SI  - GENBANK/AF052596
PT  - Journal Article
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Glucose Transporter Type 4)
RN  - 0 (Membrane Proteins)
RN  - 0 (Monosaccharide Transport Proteins)
RN  - 0 (Muscle Proteins)
RN  - 0 (Qa-SNARE Proteins)
RN  - 0 (Qb-SNARE Proteins)
RN  - 0 (Qc-SNARE Proteins)
RN  - 0 (SLC2A4 protein, human)
RN  - 0 (SNAP23 protein, human)
RN  - 0 (SNARE Proteins)
RN  - 0 (Slc2a4 protein, mouse)
RN  - 0 (Slc2a4 protein, rat)
RN  - 0 (Snap23 protein, mouse)
RN  - 0 (Vesicular Transport Proteins)
SB  - IM
MH  - Adipocytes/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Biological Transport
MH  - Blotting, Southern
MH  - Carrier Proteins/chemistry/genetics/*metabolism
MH  - Cloning, Molecular
MH  - DNA, Complementary
MH  - Glucose Transporter Type 4
MH  - Humans
MH  - Male
MH  - Membrane Proteins/*metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Monosaccharide Transport Proteins/metabolism
MH  - *Muscle Proteins
MH  - Qa-SNARE Proteins
MH  - Qb-SNARE Proteins
MH  - Qc-SNARE Proteins
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - SNARE Proteins
MH  - Sequence Homology, Amino Acid
MH  - Subcellular Fractions/metabolism
MH  - *Vesicular Transport Proteins
PMC - PMC1220107
EDAT- 1999/03/03 00:00
MHDA- 1999/03/03 00:01
CRDT- 1999/03/03 00:00
PHST- 1999/03/03 00:00 [pubmed]
PHST- 1999/03/03 00:01 [medline]
PHST- 1999/03/03 00:00 [entrez]
PST - ppublish
SO  - Biochem J. 1999 Mar 15;338 ( Pt 3):709-15.