PMID- 19161385
OWN - NLM
STAT- MEDLINE
DCOM- 20090212
LR  - 20090123
IS  - 1749-6632 (Electronic)
IS  - 0077-8923 (Linking)
VI  - 1152
DP  - 2009 Jan
TI  - SNAP-25 and gene-targeted mouse mutants.
PG  - 145-53
LID - 10.1111/j.1749-6632.2008.04009.x [doi]
AB  - The evolutionary conserved soluble N-ethylmaleimide-sensitive factor attachment 
      protein receptor (SNARE) fusion machinery is the operational unit in the release 
      of neurotransmitters and hormones from excitable cells. The SNARE core complex 
      consists of three proteins named SNAP-25 (synaptosomal-associated protein of 25 
      kD), syntaxin 1, and VAMP (vesicle-associated membrane protein)/synaptobrevin. 
      Syntaxin 1 is, together with SNAP-25, localized to the plasma membrane, whereas 
      VAMP/synaptobrevin is a component of secretory vesicles. In concert with the 
      SNAREs, accessory factors govern the docking and priming of secretory vesicles 
      prior to trans-SNARE complex formation and ultimately Ca(2+)-triggered fusion 
      pore opening at the plasma membrane. The synaptic SNAP-25 protein exists as two 
      closely related protein variants, named SNAP-25a and SNAP-25b. SNAP-25a and 
      SNAP-25b are both encoded from a single copy gene and generated by obligate 
      alternative splicing between two similar exon 5 sequences. Exon 5 spans a region 
      of SNAP-25 that is subject to posttranslational palmitoylation and implicated in 
      membrane anchoring of this cytosolic protein. The alternative splicing is 
      strictly developmentally and neuroanatomically regulated, but the biological 
      relevance of the distinct expression of these two similar protein variants is 
      still a question of debate. However, recent findings in gene-targeted mouse 
      mutants have started to unravel the importance that physiological levels of total 
      SNAP-25 protein are present and, importantly, that this is accompanied by a 
      balanced expression of SNAP-25a and SNAP-25b.
FAU - Bark, Christina
AU  - Bark C
AD  - The Rolf Luft Center for Diabetes and Endocrinology, Department of Molecular 
      Medicine and Surgery, Karolinska Institutet, Karolinska University Hospital, 
      Stockholm, Sweden. Christina.Bark@ki.se
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Ann N Y Acad Sci
JT  - Annals of the New York Academy of Sciences
JID - 7506858
RN  - 0 (Synaptosomal-Associated Protein 25)
SB  - IM
MH  - Animals
MH  - Gene Expression Regulation/genetics
MH  - Humans
MH  - Mice
MH  - Mutation/genetics
MH  - Synaptosomal-Associated Protein 25/deficiency/genetics/*metabolism
MH  - Transgenes/genetics
EDAT- 2009/01/24 09:00
MHDA- 2009/02/13 09:00
CRDT- 2009/01/24 09:00
PHST- 2009/01/24 09:00 [entrez]
PHST- 2009/01/24 09:00 [pubmed]
PHST- 2009/02/13 09:00 [medline]
AID - NYAS04009 [pii]
AID - 10.1111/j.1749-6632.2008.04009.x [doi]
PST - ppublish
SO  - Ann N Y Acad Sci. 2009 Jan;1152:145-53. doi: 10.1111/j.1749-6632.2008.04009.x.