Dystrobrevin is a protein that binds to dystrophin in the costamere of skeletal muscle cells. In humans, there are at least two isoforms of dystrobrevin, dystrobrevin alpha and dystrobrevin beta.
dystrobrevin, alpha | |||||||
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Identifiers | |||||||
Symbol | DTNA | ||||||
NCBI gene | 1837 | ||||||
HGNC | 3057 | ||||||
OMIM | 601239 | ||||||
RefSeq | NM_032981 | ||||||
UniProt | Q9Y4J8 | ||||||
Other data | |||||||
Locus | Chr. 18 q12 | ||||||
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dystrobrevin, beta | |||||||
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Identifiers | |||||||
Symbol | DTNB | ||||||
NCBI gene | 1838 | ||||||
HGNC | 3058 | ||||||
OMIM | 602415 | ||||||
RefSeq | NM_033147 | ||||||
UniProt | O60941 | ||||||
Other data | |||||||
Locus | Chr. 2 p24 | ||||||
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Dystrobrevins are members of dystrophin-related protein family which are thought to play an important role in intracellular signal transduction and provide a membrane scaffold in muscle. Defects in dystrobrevins and their associated proteins cause a range of neuromuscular diseases such as muscular dystrophies. Dystrobrevin was first identified by isolating from the electric organ of the electric ray Torpedo californica.[1] It is a phosphoprotein, which weights 87 kDa, associated with the postsynaptic membrane at the cytoplasmic face.[2][3] Dystrobrevin proteins have been said to participates in the formation and stability of synapses because it copurifies with acetylcholine receptors from Torpedo electric organ membranes.[4]
In 1997, an experiment was done using the yeast two-hybrid model to identify protein-protein interaction between dystrobrevin and dystrophin-associated protein complex (DPC). The evidence suggested that dystrobrevin works as a motor protein receptor that might play an important role in the transport of components of the dystrophin-associated protein complex to specific intracellular sites.[5] The DPC is expressed in both muscle and non-muscle tissues. It works as a mechanical component of cells and a dynamic multifunctional structure that can serve as a scaffold for signaling molecules.[6] The dystrophin-associated proteins can be divided into three groups depending on their cellular localization: extracellular, transmembrane, and cytoplasmic. Dystrobrevin protein is a part of the cytoplasmic complex and an intracellular protein that binds directly to dystrophin.
In invertebrates, dystrobrevin is present as a single protein, while in vertebrates, there are two isoforms, a-dystrobrevin (DTNA) and
Evolutionary History
editA phylogenic tree for the dystrophin protein family has been proposed based on the analysis of known dystrobrevin and dystrophin sequences that were extracted from human and fruit fly proteins.[8] The phylogeny postulated a non-metazoan ancestor that had a single dystrophin/dystrobrevin protein, which probably functioned as a homodimer. At some point before the last common ancestor of metazoans, a duplication lead to a separation of dystrophin and dystrobrevin genes, their protein products forming a heterodimer of more specialized components. In vertebrates, two other duplications occurred. The first gave rise to DRP2, a common ancestor of dystrophin and utrophin, and to
Classification
editDystrobrevins are the product of two distinct genes coding for two highly homologous proteins,
Alpha Dystrobrevin
editThe
Beta Dystrobrevins
editThe
Gene and transcripts
editThe human
The human
Structure of protein
editLocalization
editThe location and expression pattern of
Function
editThe fundamental role of the dystrobrevin protein family remains unclear. Much of what we do know has been observation from biochemical studies of associated proteins and the phenotypic consequences of their loss.
Dystrobrevins and muscle diseases
editThe consequences of null mutation are known for humans and rodents in the case of dystrophin, utrophin, and
References
edit- ^ a b Yeadon JE, Lin H, Dyer SM, Burden SJ (November 1991). "Dystrophin is a component of the subsynaptic membrane". The Journal of Cell Biology. 115 (4): 1069–76. doi:10.1083/jcb.115.4.1069. PMC 2289946. PMID 1720119.
- ^ Carr C, Fischbach GD, Cohen JB (October 1989). "A novel 87,000-Mr protein associated with acetylcholine receptors in Torpedo electric organ and vertebrate skeletal muscle". The Journal of Cell Biology. 109 (4 Pt 1): 1753–64. doi:10.1083/jcb.109.4.1753. PMC 2115790. PMID 2793938.
- ^ Butler MH, Douville K, Murnane AA, Kramarcy NR, Cohen JB, Sealock R, Froehner SC (March 1992). "Association of the Mr 58,000 postsynaptic protein of electric tissue with Torpedo dystrophin and the Mr 87,000 postsynaptic protein". The Journal of Biological Chemistry. 267 (9): 6213–8. doi:10.1016/S0021-9258(18)42683-X. PMID 1556129.
- ^ a b c Sadoulet-Puccio HM, Rajala M, Kunkel LM (November 1997). "Dystrobrevin and dystrophin: an interaction through coiled-coil motifs". Proceedings of the National Academy of Sciences of the United States of America. 94 (23): 12413–8. Bibcode:1997PNAS...9412413S. doi:10.1073/pnas.94.23.12413. PMC 24974. PMID 9356463.
- ^ Roberts RG (2001). "Dystrophins and dystrobrevins". Genome Biology. 2 (4): REVIEWS3006. doi:10.1186/gb-2001-2-4-reviews3006. PMC 138928. PMID 11305946.
- ^ a b Constantin B (February 2014). "Dystrophin complex functions as a scaffold for signalling proteins". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1838 (2): 635–42. doi:10.1016/j.bbamem.2013.08.023. PMID 24021238.
- ^ a b Blake DJ, Nawrotzki R, Loh NY, Górecki DC, Davies KE (January 1998). "beta-dystrobrevin, a member of the dystrophin-related protein family". Proceedings of the National Academy of Sciences of the United States of America. 95 (1): 241–6. Bibcode:1998PNAS...95..241B. doi:10.1073/pnas.95.1.241. PMC 18188. PMID 9419360.
- ^ Roberts RG, Bobrow M (April 1998). "Dystrophins in vertebrates and invertebrates". Human Molecular Genetics. 7 (4): 589–95. doi:10.1093/hmg/7.4.589. PMID 9499411.
- ^ Holland PW, Garcia-Fernàndez J, Williams NA, Sidow A (1994). "Gene duplications and the origins of vertebrate development". Development. 1994: 125–33. doi:10.1242/dev.1994.Supplement.125. PMID 7579513.
- ^ a b c Blake DJ, Tinsley JM, Davies KE, Knight AE, Winder SJ, Kendrick-Jones J (April 1995). "Coiled-coil regions in the carboxy-terminal domains of dystrophin and related proteins: potentials for protein-protein interactions". Trends in Biochemical Sciences. 20 (4): 133–5. doi:10.1016/s0968-0004(00)88986-0. PMID 7770909.
- ^ a b c Sadoulet-Puccio HM, Feener CA, Schaid DJ, Thibodeau SN, Michels VV, Kunkel LM (May 1997). "The genomic organization of human dystrobrevin". Neurogenetics. 1 (1): 37–42. doi:10.1007/s100480050006. PMID 10735273. S2CID 22588879.
- ^ a b c Blake DJ, Nawrotzki R, Peters MF, Froehner SC, Davies KE (March 1996). "Isoform diversity of dystrobrevin, the murine 87-kDa postsynaptic protein". The Journal of Biological Chemistry. 271 (13): 7802–10. doi:10.1074/jbc.271.13.7802. PMID 8631824.
- ^ Nawrotzki R, Loh NY, Ruegg MA, Davies KE, Blake DJ (September 1998). "Characterisation of alpha-dystrobrevin in muscle". Journal of Cell Science. 111 ( Pt 17) (17): 2595–605. doi:10.1242/jcs.111.17.2595. PMID 9701558.
- ^ Enigk RE, Maimone MM (October 1999). "Differential expression and developmental regulation of a novel alpha-dystrobrevin isoform in muscle". Gene. 238 (2): 479–88. doi:10.1016/S0378-1119(99)00358-3. PMID 10570976.
- ^ Yoshida M, Hama H, Ishikawa-Sakurai M, Imamura M, Mizuno Y, Araishi K, et al. (April 2000). "Biochemical evidence for association of dystrobrevin with the sarcoglycan-sarcospan complex as a basis for understanding sarcoglycanopathy". Human Molecular Genetics. 9 (7): 1033–40. doi:10.1093/hmg/9.7.1033. PMID 10767327.
- ^ Peters MF, Sadoulet-Puccio HM, Grady MR, Kramarcy NR, Kunkel LM, Sanes JR, et al. (September 1998). "Differential membrane localization and intermolecular associations of alpha-dystrobrevin isoforms in skeletal muscle". The Journal of Cell Biology. 142 (5): 1269–78. doi:10.1083/jcb.142.5.1269. PMC 2149339. PMID 9732287.
- ^ a b Blake DJ, Nawrotzki R, Loh NY, Górecki DC, Davies KE (January 1998). "beta-dystrobrevin, a member of the dystrophin-related protein family". Proceedings of the National Academy of Sciences of the United States of America. 95 (1): 241–6. Bibcode:1998PNAS...95..241B. doi:10.1073/pnas.95.1.241. PMC 18188. PMID 9419360.
- ^ a b Böhm SV, Roberts RG (2009). "Expression of members of the dystrophin, dystrobrevin, and dystrotelin superfamily". Critical Reviews in Eukaryotic Gene Expression. 19 (2): 89–108. doi:10.1615/critreveukargeneexpr.v19.i2.10. PMID 19392646.
- ^ Ahn AH, Freener CA, Gussoni E, Yoshida M, Ozawa E, Kunkel LM (February 1996). "The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives". The Journal of Biological Chemistry. 271 (5): 2724–30. doi:10.1074/jbc.271.5.2724. PMID 8576247.
- ^ Ahn AH, Kunkel LM (February 1995). "Syntrophin binds to an alternatively spliced exon of dystrophin". The Journal of Cell Biology. 128 (3): 363–71. doi:10.1083/jcb.128.3.363. PMC 2120343. PMID 7844150.
- ^ "About Duchenne Muscular Dystrophy". Genome.gov. Retrieved 2020-04-30.
- ^ a b Strakova J, Dean JD, Sharpe KM, Meyers TA, Odom GL, Townsend D (November 2014). "Dystrobrevin increases dystrophin's binding to the dystrophin-glycoprotein complex and provides protection during cardiac stress". Journal of Molecular and Cellular Cardiology. 76: 106–15. doi:10.1016/j.yjmcc.2014.08.013. PMC 4271192. PMID 25158611.
External links
edit- Dystrobrevin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)