Beta-synuclein

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Synuclein, beta
Identifiers
Symbols SNCB ;
External IDs Template:OMIM5 Template:MGI HomoloGene: 2320
RNA expression pattern
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

Synuclein, beta, also known as SNCB, is a human gene.[1]

The protein encoded by this gene is highly homologous to alpha-synuclein. These proteins are abundantly expressed in the brain and putatively inhibit phospholipase D2 selectively. The encoded protein, which may play a role in neuronal plasticity, is abundant in neurofibrillary lesions of patients with Alzheimer disease. This protein has been shown to be highly expressed in the substantia nigra of the brain, a region of neuronal degeneration in patients with Parkinson disease; however, no direct relation to Parkinson disease has been established. Two transcript variants encoding the same protein have been found for this gene.[1]

Beta-synuclein is a synuclein protein found primarily in brain tissue and is seen mainly in presynaptic terminals. Beta-synuclein is predominantly expressed in the neocortex, hippocampus, striatum, thalamus, and cerebellum. It is not found in Lewy bodies, but it is associated with hippocampal pathology in Parkinson's disease and dementia with Lewy bodies.[2]

Beta-synuclein is suggested to be an inhibitor of alpha-synuclein aggregation, which occurs in neurodegenerative diseases such as Parkinson's disease. Thus, beta-synuclein may protect the central nervous system from the neurotoxic effects of alpha-synuclein and provide a novel treatment of neurodegenerative disorders.[3][4]

See also

References

  1. ↑ 1.0 1.1 "Entrez Gene: SNCB synuclein, beta".
  2. ↑ George, JM. (2001) The synucleins. Genome Biology 3(1):reviews3002.1-3002.6. PMID 11806835
  3. ↑ Hashimoto M, Bar-On P, Ho G, Takenouchi T, Rockenstein E, Crews L, Masliah E. (2004) Beta-synuclein regulates Akt activity in neuronal cells. A possible neuroprotection in Parkinson's disease. J Biol Chem 279(22):23622-9. PMID 15026413
  4. ↑ Hashimoto M, Rockenstein E, Mante M, Mallory M, Masliah E. (2001) Beta-synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor. Neuron 25(2):213-223. PMID 11683992.

Further reading

  • Spillantini MG, Divane A, Goedert M (1995). "Assignment of human alpha-synuclein (SNCA) and beta-synuclein (SNCB) genes to chromosomes 4q21 and 5q35". Genomics. 27 (2): 379–81. doi:10.1006/geno.1995.1063. PMID 7558013.
  • Jakes R, Spillantini MG, Goedert M (1994). "Identification of two distinct synucleins from human brain". FEBS Lett. 345 (1): 27–32. PMID 8194594.
  • Jensen PH, Hojrup P, Hager H; et al. (1997). "Binding of Abeta to alpha- and beta-synucleins: identification of segments in alpha-synuclein/NAC precursor that bind Abeta and NAC". Biochem. J. 323 ( Pt 2): 539–46. PMID 9163350.
  • Lavedan C, Leroy E, Torres R; et al. (1999). "Genomic organization and expression of the human beta-synuclein gene (SNCB)". Genomics. 54 (1): 173–5. doi:10.1006/geno.1998.5556. PMID 9806846.
  • Pronin AN, Morris AJ, Surguchov A, Benovic JL (2000). "Synucleins are a novel class of substrates for G protein-coupled receptor kinases". J. Biol. Chem. 275 (34): 26515–22. doi:10.1074/jbc.M003542200. PMID 10852916.
  • Rockenstein E, Hansen LA, Mallory M; et al. (2001). "Altered expression of the synuclein family mRNA in Lewy body and Alzheimer's disease". Brain Res. 914 (1–2): 48–56. PMID 11578596.
  • Tanji K, Mori F, Nakajo S; et al. (2001). "Expression of beta-synuclein in normal human astrocytes". Neuroreport. 12 (13): 2845–8. PMID 11588588.
  • Hashimoto M, Rockenstein E, Mante M; et al. (2001). "beta-Synuclein inhibits alpha-synuclein aggregation: a possible role as an anti-parkinsonian factor". Neuron. 32 (2): 213–23. PMID 11683992.
  • Uversky VN, Li J, Souillac P; et al. (2002). "Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins". J. Biol. Chem. 277 (14): 11970–8. doi:10.1074/jbc.M109541200. PMID 11812782.
  • 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.
  • Ihara M, Tomimoto H, Kitayama H; et al. (2003). "Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies". J. Biol. Chem. 278 (26): 24095–102. doi:10.1074/jbc.M301352200. PMID 12695511.
  • Fung KM, Rorke LB, Giasson B; et al. (2003). "Expression of alpha-, beta-, and gamma-synuclein in glial tumors and medulloblastomas". Acta Neuropathol. 106 (2): 167–75. doi:10.1007/s00401-003-0718-x. PMID 12783249.
  • da Costa CA, Masliah E, Checler F (2003). "Beta-synuclein displays an antiapoptotic p53-dependent phenotype and protects neurons from 6-hydroxydopamine-induced caspase 3 activation: cross-talk with alpha-synuclein and implication for Parkinson's disease". J. Biol. Chem. 278 (39): 37330–5. doi:10.1074/jbc.M306083200. PMID 12867415.
  • Ohtake H, Limprasert P, Fan Y; et al. (2005). "Beta-synuclein gene alterations in dementia with Lewy bodies". Neurology. 63 (5): 805–11. PMID 15365127.
  • 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.
  • Snyder H, Mensah K, Hsu C; et al. (2005). "beta-Synuclein reduces proteasomal inhibition by alpha-synuclein but not gamma-synuclein". J. Biol. Chem. 280 (9): 7562–9. doi:10.1074/jbc.M412887200. PMID 15591046.
  • Sung YH, Eliezer D (2006). "Secondary structure and dynamics of micelle bound beta- and gamma-synuclein". Protein Sci. 15 (5): 1162–74. doi:10.1110/ps.051803606. PMID 16597821.
  • Fan Y, Limprasert P, Murray IV; et al. (2006). "Beta-synuclein modulates alpha-synuclein neurotoxicity by reducing alpha-synuclein protein expression". Hum. Mol. Genet. 15 (20): 3002–11. doi:10.1093/hmg/ddl242. PMID 16959793.
  • Myslinski E, Gérard MA, Krol A, Carbon P (2007). "A genome scale location analysis of human Staf/ZNF143-binding sites suggests a widespread role for human Staf/ZNF143 in mammalian promoters". J. Biol. Chem. 281 (52): 39953–62. doi:10.1074/jbc.M608507200. PMID 17092945.
  • Sung YH, Eliezer D (2007). "Residual structure, backbone dynamics, and interactions within the synuclein family". J. Mol. Biol. 372 (3): 689–707. doi:10.1016/j.jmb.2007.07.008. PMID 17681534.
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