PMID- 10625663
OWN - NLM
STAT- MEDLINE
DCOM- 20000218
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 2
DP  - 2000 Jan 14
TI  - SNIP, a novel SNAP-25-interacting protein implicated in regulated exocytosis.
PG  - 1191-200
AB  - Synaptosome-associated protein of 25 kDa (SNAP-25) is a presynaptic membrane
      protein that has been clearly implicated in membrane fusion in both developing
      and mature neurons, although its mechanisms of action are unclear. We have now
      identified a novel SNAP-25-interacting protein named SNIP. SNIP is a hydrophilic,
      145-kDa protein that comprises two predicted coiled-coil domains, two highly
      charged regions, and two proline-rich domains with multiple PPXY and PXXP motifs.
      SNIP is selectively expressed in brain where it co-distributes with SNAP-25 in
      most brain regions. Biochemical studies have revealed that SNIP is tightly
      associated with the brain cytoskeleton. Subcellular fractionation and
      immunofluorescence localization studies have demonstrated that SNIP co-localizes 
      with SNAP-25 as well as the cortical actin cytoskeleton, suggesting that SNIP
      serves as a linker protein connecting SNAP-25 to the submembranous cytoskeleton. 
      By using deletion analysis, we have mapped the binding domains of SNIP and
      SNAP-25, and we have demonstrated that the SNIP-SNAP-25 association is mediated
      via coiled-coil interactions. Moreover, we have shown that overexpression of SNIP
      or its SNAP-25-interacting domain inhibits Ca(2+)-dependent exocytosis from PC12 
      cells. These results indicate that SNIP is involved in regulation of
      neurosecretion, perhaps via its interaction with SNAP-25 and the cytoskeleton.
FAU - Chin, L S
AU  - Chin LS
AD  - Departments of Pharmacology and Physiology, Bowles Center for Alcohol Studies,
      School of Medicine, University of North Carolina, Chapel Hill, North Carolina
      27599, USA.
FAU - Nugent, R D
AU  - Nugent RD
FAU - Raynor, M C
AU  - Raynor MC
FAU - Vavalle, J P
AU  - Vavalle JP
FAU - Li, L
AU  - Li L
LA  - eng
SI  - GENBANK/AF156981
SI  - GENBANK/AF156982
GR  - NS37939/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Adaptor Proteins, Vesicular Transport)
RN  - 0 (Carrier Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Snap25 protein, rat)
RN  - 0 (Srcin1 protein, rat)
RN  - 0 (Synaptosomal-Associated Protein 25)
RN  - 0 (Vesicular Transport Proteins)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Adaptor Proteins, Vesicular Transport
MH  - Amino Acid Sequence
MH  - Animals
MH  - Brain/*metabolism
MH  - Calcium/metabolism
MH  - Carrier Proteins/chemistry/genetics/*metabolism
MH  - Cloning, Molecular
MH  - Exocytosis/*physiology
MH  - Gene Expression Regulation
MH  - Gene Library
MH  - Hippocampus/metabolism
MH  - *Membrane Proteins
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Nerve Tissue Proteins/chemistry/genetics/*metabolism
MH  - Organ Specificity
MH  - PC12 Cells
MH  - Protein Conformation
MH  - Protein Structure, Secondary
MH  - Rats
MH  - Recombinant Proteins/biosynthesis/chemistry
MH  - Subcellular Fractions/metabolism
MH  - Synaptosomal-Associated Protein 25
MH  - Transfection
MH  - *Vesicular Transport Proteins
EDAT- 2000/01/08 09:00
MHDA- 2000/02/26 09:00
CRDT- 2000/01/08 09:00
PHST- 2000/01/08 09:00 [pubmed]
PHST- 2000/02/26 09:00 [medline]
PHST- 2000/01/08 09:00 [entrez]
AID - 10.1074/jbc.275.2.1191 [doi]
AID - S0021-9258(18)31235-3 [pii]
PST - ppublish
SO  - J Biol Chem. 2000 Jan 14;275(2):1191-200. doi: 10.1074/jbc.275.2.1191.