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Tubulin beta-4A chain is a protein that in humans is encoded by the TUBB4Agene. Two tubulin beta-4 chain proteins are encoded in the human genome by the genes TUBB4A (this entry) and TUBB4B.[1][2][3] Tubulin is the major constituent of microtubules, a key components of the cytoskeleton. It binds two moles of GTP, one at an exchangeable site on the beta-chain and one at a non-exchangeable site on the alpha-chain. TUBB4A is preferentially and highly expressed in the central nervous system.[4]
Mutations in TUBB4A have been associated with two neurological disorders.
An R2G substitution in the autoregulatory MREI domain of TUBB4A has been identified as the cause of 'hereditary whispering dysphonia' or DYT4.[5][6]
A de novo D249N mutation has been identified as the cause of a rare leukoencephalopathy, hypomyelination with atrophy of the basal ganglia and cerebellum (H-ABC).[7][8]
↑Shimojima, K; Okumura, A; Ikeno, M; Nishimura, A; Saito, A; Saitsu, H; Matsumoto, N; Yamamoto, T (2014). "A de novo TUBB4A mutation in a patient with hypomyelination mimicking Pelizaeus-Merzbacher disease". Brain & Development. 37: 281–285. doi:10.1016/j.braindev.2014.05.004. PMID24974158.
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Tarazona R, López-Lluch G, Galiani MD, et al. (2001). "HLA-B2702 (77-83/83-77) peptide binds to beta-tubulin on human NK cells and blocks their cytotoxic capacity". Journal of Immunology. 165 (12): 6776–6782. doi:10.4049/jimmunol.165.12.6776. PMID11120798.
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Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nature Genetics. 36 (1): 40–45. doi:10.1038/ng1285. PMID14702039.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID14743216.
Hassel S, Eichner A, Yakymovych M, et al. (2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel electrophoresis and mass spectrometry". Proteomics. 4 (5): 1346–1358. doi:10.1002/pmic.200300770. PMID15188402.
Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–1450. doi:10.1016/j.cub.2004.07.051. PMID15324660.
Campbell GR, Pasquier E, Watkins J, et al. (2005). "The glutamine-rich region of the HIV-1 Tat protein is involved in T-cell apoptosis". Journal of Biological Chemistry. 279 (46): 48197–48204. doi:10.1074/jbc.M406195200. PMID15331610.
Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–126. doi:10.1093/dnares/12.2.117. PMID16303743.
Coiras M, Camafeita E, Ureña T, et al. (2006). "Modifications in the human T cell proteome induced by intracellular HIV-1 Tat protein expression". Proteomics. 6 Suppl 1: S63–7S3. doi:10.1002/pmic.200500437. PMID16526095.
