Beta-synuclein

SNCB
Identifiers
AliasesSNCB, entrez:6620, synuclein beta
External IDsOMIM: 602569; MGI: 1889011; HomoloGene: 2320; GeneCards: SNCB; OMA:SNCB - orthologs
Orthologs
SpeciesHumanMouse
Entrez

6620

104069

Ensembl

ENSG00000074317

ENSMUSG00000034891

UniProt

Q16143

Q91ZZ3

RefSeq (mRNA)

NM_033610
NM_001362407

RefSeq (protein)

NP_291088
NP_001349336

Location (UCSC)Chr 5: 176.62 – 176.63 MbChr 13: 54.91 – 54.91 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Beta-synuclein is a protein that in humans is encoded by the SNCB gene.[5][6][7]

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's 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's disease; however, no direct relation to Parkinson's disease has been established. Two transcript variants encoding the same protein have been found for this gene.[7]

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 PD and DLB.[8]

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.[9][10]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000074317 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000034891 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Spillantini MG, Divane A, Goedert M (Nov 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.
  6. ^ Lavedan C, Leroy E, Torres R, Dehejia A, Dutra A, Buchholtz S, Nussbaum RL, Polymeropoulos MH (Jan 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.
  7. ^ a b "Entrez Gene: SNCB synuclein, beta".
  8. ^ George, JM (2002). "The synucleins". Genome Biology. 3 (1): REVIEWS3002. doi:10.1186/gb-2001-3-1-reviews3002. PMC 150459. PMID 11806835.
  9. ^ 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 mechanism for neuroprotection in Parkinson's disease". The Journal of Biological Chemistry. 279 (22): 23622–9. doi:10.1074/jbc.M313784200. PMID 15026413.
  10. ^ 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. 32 (2): 213–23. doi:10.1016/S0896-6273(01)00462-7. PMID 11683992. S2CID 14766899.

Further reading

  • Jakes R, Spillantini MG, Goedert M (1994). "Identification of two distinct synucleins from human brain". FEBS Lett. 345 (1): 27–32. doi:10.1016/0014-5793(94)00395-5. PMID 8194594. S2CID 36840279.
  • 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. doi:10.1042/bj3230539. PMC 1218353. PMID 9163350.
  • 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. doi:10.1016/S0006-8993(01)02772-X. PMID 11578596. S2CID 35448948.
  • Tanji K, Mori F, Nakajo S, et al. (2001). "Expression of beta-synuclein in normal human astrocytes". NeuroReport. 12 (13): 2845–8. doi:10.1097/00001756-200109170-00018. PMID 11588588. S2CID 84671534.
  • 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. doi:10.1016/S0896-6273(01)00462-7. PMID 11683992. S2CID 14766899.
  • 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. S2CID 39712533.
  • 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). "β-Synuclein gene alterations in dementia with Lewy bodies". Neurology. 63 (5): 805–11. doi:10.1212/01.wnl.0000139870.14385.3c. PMC 1808539. 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. PMC 528928. 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 β- and γ-synuclein". Protein Sci. 15 (5): 1162–74. doi:10.1110/ps.051803606. PMC 2242515. 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. PMC 2094134. PMID 17681534.

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