TUBA4A
Tubulin alpha-4A chain is a protein that in humans is encoded by the TUBA4A gene.[1]
Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulin. The genes encoding these microtubule constituents are part of the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes and they are highly conserved among and between species. This gene encodes an alpha tubulin that is a highly conserved homolog of a rat testis-specific alpha tubulin.[2]
Interactions
TUBA4A has been shown to interact with NCOA6[3] and APC.[4]
References
- ^ Villasante A, Wang D, Dobner P, Dolph P, Lewis SA, Cowan NJ (Jan 1987). "Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis-specific expression of two sister genes". Mol Cell Biol 6 (7): 2409–19. PMC 367794. PMID 3785200. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=367794.
- ^ "Entrez Gene: TUBA4A tubulin, alpha 4a". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7277.
- ^ Goo, Young-Hwa; Sohn Young Chang, Kim Dae-Hwan, Kim Seung-Whan, Kang Min-Jung, Jung Dong-Ju, Kwak Eunyee, Barlev Nickolai A, Berger Shelley L, Chow Vincent T, Roeder Robert G, Azorsa David O, Meltzer Paul S, Suh Pan-Gil, Song Eun Joo, Lee Kong-Joo, Lee Young Chul, Lee Jae Woon (Jan. 2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. (United States) 23 (1): 140–9. doi:10.1128/MCB.23.1.140-149.2003. ISSN 0270-7306. PMC 140670. PMID 12482968. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=140670.
- ^ Zumbrunn, J; Kinoshita K, Hyman A A, Näthke I S (Jan. 2001). "Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3 beta phosphorylation". Curr. Biol. (England) 11 (1): 44–9. doi:10.1016/S0960-9822(01)00002-1. ISSN 0960-9822. PMID 11166179.
Further reading
- Desai A, Mitchison TJ (1998). "Tubulin and FtsZ structures: functional and therapeutic implications.". Bioessays 20 (7): 523–7. doi:10.1002/(SICI)1521-1878(199807)20:7<523::AID-BIES1>3.0.CO;2-L. PMID 9722999.
- Oakley BR (2001). "An abundance of tubulins.". Trends Cell Biol. 10 (12): 537–42. doi:10.1016/S0962-8924(00)01857-2. PMID 11121746.
- Dutcher SK (2001). "The tubulin fraternity: alpha to eta.". Curr. Opin. Cell Biol. 13 (1): 49–54. doi:10.1016/S0955-0674(00)00173-3. PMID 11163133.
- Kirsch J, Langosch D, Prior P, et al. (1991). "The 93-kDa glycine receptor-associated protein binds to tubulin.". J. Biol. Chem. 266 (33): 22242–5. PMID 1657993.
- Dobner PR, Kislauskis E, Wentworth BM, Villa-Komaroff L (1987). "Alternative 5' exons either provide or deny an initiator methionine codon to the same alpha-tubulin coding region.". Nucleic Acids Res. 15 (1): 199–218. doi:10.1093/nar/15.1.199. PMC 340405. PMID 3029670. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=340405.
- Hall JL, Cowan NJ (1985). "Structural features and restricted expression of a human alpha-tubulin gene.". Nucleic Acids Res. 13 (1): 207–23. doi:10.1093/nar/13.1.207. PMC 340985. PMID 3839072. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=340985.
- Alexandrova N, Niklinski J, Bliskovsky V, et al. (1995). "The N-terminal domain of c-Myc associates with alpha-tubulin and microtubules in vivo and in vitro.". Mol. Cell. Biol. 15 (9): 5188–95. PMC 230766. PMID 7651436. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=230766.
- Yamaguchi N, Fukuda MN (1995). "Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins.". J. Biol. Chem. 270 (20): 12170–6. doi:10.1074/jbc.270.33.19551. PMID 7744867.
- Waterman-Storer CM, Karki S, Holzbaur EL (1995). "The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1).". Proc. Natl. Acad. Sci. U.S.A. 92 (5): 1634–8. doi:10.1073/pnas.92.5.1634. PMC 42574. PMID 7878030. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=42574.
- Lu Q, Luduena RF (1994). "In vitro analysis of microtubule assembly of isotypically pure tubulin dimers. Intrinsic differences in the assembly properties of alpha beta II, alpha beta III, and alpha beta IV tubulin dimers in the absence of microtubule-associated proteins.". J. Biol. Chem. 269 (3): 2041–7. PMID 8294455.
- Paschal BM, Holzbaur EL, Pfister KK, et al. (1993). "Characterization of a 50-kDa polypeptide in cytoplasmic dynein preparations reveals a complex with p150GLUED and a novel actin.". J. Biol. Chem. 268 (20): 15318–23. PMID 8325901.
- Huby RD, Carlile GW, Ley SC (1996). "Interactions between the protein-tyrosine kinase ZAP-70, the proto-oncoprotein Vav, and tubulin in Jurkat T cells.". J. Biol. Chem. 270 (51): 30241–4. doi:10.1074/jbc.270.51.30241. PMID 8530437.
- Marie-Cardine A, Kirchgessner H, Eckerskorn C, et al. (1996). "Human T lymphocyte activation induces tyrosine phosphorylation of alpha-tubulin and its association with the SH2 domain of the p59fyn protein tyrosine kinase.". Eur. J. Immunol. 25 (12): 3290–7. doi:10.1002/eji.1830251214. PMID 8566014.
- Peters JD, Furlong MT, Asai DJ, et al. (1996). "Syk, activated by cross-linking the B-cell antigen receptor, localizes to the cytosol where it interacts with and phosphorylates alpha-tubulin on tyrosine.". J. Biol. Chem. 271 (9): 4755–62. doi:10.1074/jbc.271.9.4755. PMID 8617742.
- Best A, Ahmed S, Kozma R, Lim L (1996). "The Ras-related GTPase Rac1 binds tubulin.". J. Biol. Chem. 271 (7): 3756–62. doi:10.1074/jbc.271.7.3756. PMID 8631991.
- Tokito MK, Howland DS, Lee VM, Holzbaur EL (1997). "Functionally distinct isoforms of dynactin are expressed in human neurons.". Mol. Biol. Cell 7 (8): 1167–80. PMC 275970. PMID 8856662. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=275970.
- Tian G, Lewis SA, Feierbach B, et al. (1997). "Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors.". J. Cell Biol. 138 (4): 821–32. doi:10.1083/jcb.138.4.821. PMC 2138046. PMID 9265649. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2138046.
- Vaillant AR, Müller R, Langkopf A, Brown DL (1998). "Characterization of the microtubule-binding domain of microtubule-associated protein 1A and its effects on microtubule dynamics.". J. Biol. Chem. 273 (22): 13973–81. doi:10.1074/jbc.273.22.13973. PMID 9593747.
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PDB gallery
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1ffx: TUBULIN:STATHMIN-LIKE DOMAIN COMPLEX
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1ia0: KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM
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1jff: Refined structure of alpha-beta tubulin from zinc-induced sheets stabilized with taxol
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1sa0: TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX
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1sa1: Tubulin-podophyllotoxin: stathmin-like domain complex
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1tub: TUBULIN ALPHA-BETA DIMER, ELECTRON DIFFRACTION
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1tvk: The binding mode of epothilone A on a,b-tubulin by electron crystallography
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1z2b: Tubulin-colchicine-vinblastine: stathmin-like domain complex
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2hxf: KIF1A head-microtubule complex structure in amppnp-form
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2hxh: KIF1A head-microtubule complex structure in adp-form
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.