Synucleins are a family of soluble proteins common to vertebrates, primarily expressed in neural tissue and in certain tumors.[1]
| Synuclein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Synuclein | ||||||||
| Pfam | PF01387 | ||||||||
| InterPro | IPR001058 | ||||||||
| SCOP2 | 1xq8 / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 150 | ||||||||
| OPM protein | 1xq8 | ||||||||
| |||||||||
The name is a blend of the words "synapse" and "nucleus", as it was first found in the synapses in the electromotor nucleus of the electric ray.[2]
Family members
editThe synuclein family includes three known proteins: alpha-synuclein, beta-synuclein, and gamma-synuclein. Interest in the synuclein family began when alpha-synuclein was found to be mutated in several families with autosomal dominant Parkinson's disease.[3]
All synucleins have in common a highly conserved alpha-helical lipid-binding motif with similarity to the class-A2 lipid-binding domains of the exchangeable apolipoproteins. Synuclein family members are not found outside vertebrates, although they have some conserved structural similarity with plant 'late-embryo-abundant' proteins.[1]
Function
editNormal cellular functions have not been determined for any of the synuclein proteins. Some data suggest a role in the regulation of membrane stability and/or turnover.[4] Mutations in alpha-synuclein are associated with early-onset familial Parkinson's disease and the protein aggregates abnormally in Parkinson's disease, Lewy body disease, and other neurodegenerative diseases.[5][6] The gamma-synuclein protein's expression in breast tumors is a marker for tumor progression.[7][8]
Human proteins containing this domain
editReferences
edit- ^ a b George JM (2002). "The synucleins". Genome Biol. 3 (1): REVIEWS3002. doi:10.1186/gb-2001-3-1-reviews3002. PMC 150459. PMID 11806835.
- ^ SYNUCLEIN | Definition of SYNUCLEIN by Oxford Dictionary on Lexico.com
- ^ Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, Dutra A, et al. (1997). "Mutation in the alpha-synuclein gene identified in families with Parkinson's disease". Science. 276 (5321): 2045–7. doi:10.1126/science.276.5321.2045. PMID 9197268.
- ^ Kara E (2021). "An integrated genomic approach to dissect the genetic landscape regulating the cell-to-cell transfer of α-synuclein". Cell Reports. 35 (10): 109189. doi:10.1016/j.celrep.2021.109189. PMC 8207177. PMID 34107263.
- ^ Mezey E, Dehejia A, Harta G, Papp MI, Polymeropoulos MH, Brownstein MJ (1998). "Alpha synuclein in neurodegenerative disorders: murderer or accomplice?". Nat Med. 4 (7): 755–7. doi:10.1038/nm0798-755. PMID 9662355. S2CID 46196799.
- ^ Goedert M (July 2001). "Alpha-synuclein and neurodegenerative diseases". Nat. Rev. Neurosci. 2 (7): 492–501. doi:10.1038/35081564. PMID 11433374. S2CID 2792701.
- ^ Ji H, Liu YE, Jia T, Wang M, Liu J, Xiao G, et al. (1997). "Identification of a breast cancer-specific gene, BCSG1, by direct differential cDNA sequencing". Cancer Res. 57 (4): 759–64. PMID 9044857.
- ^ Bruening W, Giasson BI, Klein-Szanto AJ, Lee VM, Trojanowski JQ, Godwin AK (May 2000). "Synucleins are expressed in the majority of breast and ovarian carcinomas and in preneoplastic lesions of the ovary". Cancer. 88 (9): 2154–63. doi:10.1002/(SICI)1097-0142(20000501)88:9<2154::AID-CNCR23>3.0.CO;2-9. PMID 10813729.
External links
edit- Synucleins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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