NAPA (gene)

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N-ethylmaleimide-sensitive factor attachment protein, alpha
Identifiers
Symbols NAPA ; SNAPA
External IDs Template:OMIM5 Template:MGI HomoloGene2839
RNA expression pattern
File:PBB GE NAPA 206491 s at tn.png
File:PBB GE NAPA 208751 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

N-ethylmaleimide-sensitive factor attachment protein, alpha, also known as NAPA, is a human gene.[1]

The 'SNARE hypothesis' is a model explaining the process of docking and fusion of vesicles to their target membranes. According to this model, membrane proteins from the vesicle (v-SNAREs) and proteins from the target membrane (t-SNAREs) govern the specificity of vesicle targeting and docking through mutual recognition. Once the 2 classes of SNAREs bind to each other, they form a complex that recruits the general elements of the fusion apparatus, namely NSF (N-ethylmaleimide-sensitive factor) and SNAPs (soluble NSF-attachment proteins), to the site of membrane fusion, thereby forming the 20S fusion complex. Alpha- and gamma-SNAP are found in a wide range of tissues and act synergistically in intra-Golgi transport. The sequence of the predicted 295-amino acid human protein encoded by NAPA shares 37%, 60%, and 67% identity with the sequences of yeast, Drosophila, and squid alpha-SNAP, respectively. Platelets contain some of the same proteins, including NSF, p115/TAP, alpha-SNAP, gamma-SNAP, and the t-SNAREs syntaxin-2 and syntaxin-4, that are used in many vesicular transport processes in other cell types. Platelet exocytosis uses a molecular mechanism similar to that used by other secretory cells, such as neurons, although the proteins used by the platelet and their modes of regulation may be quite different.[1]

References

  1. 1.0 1.1 "Entrez Gene: NAPA N-ethylmaleimide-sensitive factor attachment protein, alpha".

Further reading

  • Wilson DW, Whiteheart SW, Wiedmann M; et al. (1992). "A multisubunit particle implicated in membrane fusion". J. Cell Biol. 117 (3): 531–8. PMID 1315316.
  • Whiteheart SW, Brunner M, Wilson DW; et al. (1992). "Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAP receptor complex in Golgi membranes". J. Biol. Chem. 267 (17): 12239–43. PMID 1601890.
  • Hanson PI, Otto H, Barton N, Jahn R (1995). "The N-ethylmaleimide-sensitive fusion protein and alpha-SNAP induce a conformational change in syntaxin". J. Biol. Chem. 270 (28): 16955–61. PMID 7622514.
  • Whiteheart SW, Griff IC, Brunner M; et al. (1993). "SNAP family of NSF attachment proteins includes a brain-specific isoform". Nature. 362 (6418): 353–5. doi:10.1038/362353a0. PMID 8455721.
  • Timmers KI, Clark AE, Omatsu-Kanbe M; et al. (1997). "Identification of SNAP receptors in rat adipose cell membrane fractions and in SNARE complexes co-immunoprecipitated with epitope-tagged N-ethylmaleimide-sensitive fusion protein". Biochem. J. 320 ( Pt 2): 429–36. PMID 8973549.
  • Lemons PP, Chen D, Bernstein AM; et al. (1997). "Regulated secretion in platelets: identification of elements of the platelet exocytosis machinery". Blood. 90 (4): 1490–500. PMID 9269766.
  • Subramaniam VN, Loh E, Hong W (1997). "N-Ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment proteins (SNAP) mediate dissociation of GS28-syntaxin 5 Golgi SNAP receptors (SNARE) complex". J. Biol. Chem. 272 (41): 25441–4. PMID 9325254.
  • Lowe SL, Peter F, Subramaniam VN; et al. (1997). "A SNARE involved in protein transport through the Golgi apparatus". Nature. 389 (6653): 881–4. doi:10.1038/39923. PMID 9349823.
  • Barnard RJ, Morgan A, Burgoyne RD (1997). "Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis". J. Cell Biol. 139 (4): 875–83. PMID 9362506.
  • Wong SH, Xu Y, Zhang T, Hong W (1998). "Syntaxin 7, a novel syntaxin member associated with the early endosomal compartment". J. Biol. Chem. 273 (1): 375–80. PMID 9417091.
  • Tang BL, Tan AE, Lim LK; et al. (1998). "Syntaxin 12, a member of the syntaxin family localized to the endosome". J. Biol. Chem. 273 (12): 6944–50. PMID 9507000.
  • Wong SH, Zhang T, Xu Y; et al. (1998). "Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially associated with the early endosome". Mol. Biol. Cell. 9 (6): 1549–63. PMID 9614193.
  • Osten P, Srivastava S, Inman GJ; et al. (1998). "The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs". Neuron. 21 (1): 99–110. PMID 9697855.
  • Prekeris R, Klumperman J, Chen YA, Scheller RH (1998). "Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes". J. Cell Biol. 143 (4): 957–71. PMID 9817754.
  • Nagamatsu S, Watanabe T, Nakamichi Y; et al. (1999). "alpha-soluble N-ethylmaleimide-sensitive factor attachment protein is expressed in pancreatic beta cells and functions in insulin but not gamma-aminobutyric acid secretion". J. Biol. Chem. 274 (12): 8053–60. PMID 10075705.
  • Subramaniam VN, Loh E, Horstmann H; et al. (2000). "Preferential association of syntaxin 8 with the early endosome". J. Cell. Sci. 113 ( Pt 6): 997–1008. PMID 10683148.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Hirose H, Arasaki K, Dohmae N; et al. (2005). "Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi". EMBO J. 23 (6): 1267–78. doi:10.1038/sj.emboj.7600135. PMID 15029241.
  • Singh BB, Lockwich TP, Bandyopadhyay BC; et al. (2004). "VAMP2-dependent exocytosis regulates plasma membrane insertion of TRPC3 channels and contributes to agonist-stimulated Ca2+ influx". Mol. Cell. 15 (4): 635–46. doi:10.1016/j.molcel.2004.07.010. PMID 15327778.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.

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