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Gene Review

TUBA1B  -  tubulin, alpha 1b

Homo sapiens

Synonyms: K-ALPHA-1
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Disease relevance of TUBA1B


Psychiatry related information on TUBA1B


High impact information on TUBA1B


Biological context of TUBA1B


Anatomical context of TUBA1B

  • The microtubule subunits are heterodimers composed of one alpha-tubulin polypeptide and one beta-tubulin polypeptide that should undergo a complex folding processing before they achieve a quaternary structure that will allow their incorporation into the polymer [17].
  • Two other cytoskeletal proteins, beta-actin and alpha-tubulin, clustered at the cell leading edge and uropod, respectively, of polarized lymphocytes [18].
  • We found that the cMyc mRNA was associated with a number of ribosomes comparable to that associated with alpha tubulin mRNA in all the cell lines tested [19].
  • Since polysome size is a function of the length of the translated sequence as well as the rate of initiation of protein synthesis, we also determined the number of ribosomes associated with a control mRNA (alpha tubulin) which codes for a protein of similar size to cMyc [19].
  • Force enhanced recruitment of alpha-tubulin and the plus end microtubule-binding protein cytoplasmic linker protein-170 (CLIP-170) at focal adhesions [20].

Associations of TUBA1B with chemical compounds


Regulatory relationships of TUBA1B


Other interactions of TUBA1B


Analytical, diagnostic and therapeutic context of TUBA1B


  1. Induction of cytoskeletal gene expression by insulin. Messina, J.L. Mol. Endocrinol. (1992) [Pubmed]
  2. Expression of beta-actin and alpha-tubulin mRNA in gerbil brain following transient ischemia and reperfusion up to 1 month. Kumar, K., Wu, X.L. Brain Res. Mol. Brain Res. (1995) [Pubmed]
  3. Antitumor effect of 2-methoxyestradiol in a rat orthotopic brain tumor model. Kang, S.H., Cho, H.T., Devi, S., Zhang, Z., Escuin, D., Liang, Z., Mao, H., Brat, D.J., Olson, J.J., Simons, J.W., Lavallee, T.M., Giannakakou, P., Van Meir, E.G., Shim, H. Cancer Res. (2006) [Pubmed]
  4. Expression of a human alpha-tubulin: properties of the isolated subunit. Yaffe, M.B., Levison, B.S., Szasz, J., Sternlicht, H. Biochemistry (1988) [Pubmed]
  5. Normal and prostate cancer cells display distinct molecular profiles of alpha-tubulin posttranslational modifications. Soucek, K., Kamaid, A., Phung, A.D., Kubala, L., Bulinski, J.C., Harper, R.W., Eiserich, J.P. Prostate (2006) [Pubmed]
  6. Reduction of acetylated alpha-tubulin immunoreactivity in neurofibrillary tangle-bearing neurons in Alzheimer's disease. Hempen, B., Brion, J.P. J. Neuropathol. Exp. Neurol. (1996) [Pubmed]
  7. Isolation rearing induces recognition memory deficits accompanied by cytoskeletal alterations in rat hippocampus. Bianchi, M., Fone, K.F., Azmi, N., Heidbreder, C.A., Hagan, J.J., Marsden, C.A. Eur. J. Neurosci. (2006) [Pubmed]
  8. Key interaction modes of dynamic +TIP networks. Honnappa, S., Okhrimenko, O., Jaussi, R., Jawhari, H., Jelesarov, I., Winkler, F.K., Steinmetz, M.O. Mol. Cell (2006) [Pubmed]
  9. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. North, B.J., Marshall, B.L., Borra, M.T., Denu, J.M., Verdin, E. Mol. Cell (2003) [Pubmed]
  10. Delta-tubulin and epsilon-tubulin: two new human centrosomal tubulins reveal new aspects of centrosome structure and function. Chang, P., Stearns, T. Nat. Cell Biol. (2000) [Pubmed]
  11. Defective brain microtubule assembly in Alzheimer's disease. Iqbal, K., Grundke-Iqbal, I., Zaidi, T., Merz, P.A., Wen, G.Y., Shaikh, S.S., Wisniewski, H.M., Alafuzoff, I., Winblad, B. Lancet (1986) [Pubmed]
  12. Minus-end capture of preformed kinetochore fibers contributes to spindle morphogenesis. Khodjakov, A., Copenagle, L., Gordon, M.B., Compton, D.A., Kapoor, T.M. J. Cell Biol. (2003) [Pubmed]
  13. Expression of human alpha-tubulin genes: interspecies conservation of 3' untranslated regions. Cowan, N.J., Dobner, P.R., Fuchs, E.V., Cleveland, D.W. Mol. Cell. Biol. (1983) [Pubmed]
  14. Prefoldin recognition motifs in the nonhomologous proteins of the actin and tubulin families. Rommelaere, H., De Neve, M., Neirynck, K., Peelaers, D., Waterschoot, D., Goethals, M., Fraeyman, N., Vandekerckhove, J., Ampe, C. J. Biol. Chem. (2001) [Pubmed]
  15. Histone deacetylase HDAC8 associates with smooth muscle alpha-actin and is essential for smooth muscle cell contractility. Waltregny, D., Glénisson, W., Tran, S.L., North, B.J., Verdin, E., Colige, A., Castronovo, V. FASEB J. (2005) [Pubmed]
  16. Site-directed mutagenesis of alpha-tubulin. Reductive methylation studies of the Lys 394 region. Szasz, J., Yaffe, M.B., Sternlicht, H. Biophys. J. (1993) [Pubmed]
  17. Review: postchaperonin tubulin folding cofactors and their role in microtubule dynamics. Lopez-Fanarraga, M., Avila, J., Guasch, A., Coll, M., Zabala, J.C. J. Struct. Biol. (2001) [Pubmed]
  18. Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization. Serrador, J.M., Alonso-Lebrero, J.L., del Pozo, M.A., Furthmayr, H., Schwartz-Albiez, R., Calvo, J., Lozano, F., Sánchez-Madrid, F. J. Cell Biol. (1997) [Pubmed]
  19. Translational efficiency of cMyc mRNA in Burkitt lymphoma cells. Nilsen, T.W., Maroney, P.A. Mol. Cell. Biol. (1984) [Pubmed]
  20. Regulation of tension-induced mechanotranscriptional signals by the microtubule network in fibroblasts. D'Addario, M., Arora, P.D., Ellen, R.P., McCulloch, C.A. J. Biol. Chem. (2003) [Pubmed]
  21. Posttranslational nitrotyrosination of alpha-tubulin induces cell cycle arrest and inhibits proliferation of vascular smooth muscle cells. Phung, A.D., Soucek, K., Kubala, L., Harper, R.W., Chlo?? Bulinski, J., Eiserich, J.P. Eur. J. Cell Biol. (2006) [Pubmed]
  22. Microtubules containing acetylated alpha-tubulin in mammalian cells in culture. Piperno, G., LeDizet, M., Chang, X.J. J. Cell Biol. (1987) [Pubmed]
  23. A non-canonical genetic code in an early diverging eukaryotic lineage. Keeling, P.J., Doolittle, W.F. EMBO J. (1996) [Pubmed]
  24. NPA binding activity is peripheral to the plasma membrane and is associated with the cytoskeleton. Cox, D.N., Muday, G.K. Plant Cell (1994) [Pubmed]
  25. Dissecting the cellular functions of annexin XI using recombinant human annexin XI-specific autoantibodies cloned by phage display. Farnaes, L., Ditzel, H.J. J. Biol. Chem. (2003) [Pubmed]
  26. Gene expression studies in prostate cancer tissue: which reference gene should be selected for normalization? Ohl, F., Jung, M., Xu, C., Stephan, C., Rabien, A., Burkhardt, M., Nitsche, A., Kristiansen, G., Loening, S.A., Radonić, A., Jung, K. J. Mol. Med. (2005) [Pubmed]
  27. Selective toxicity of vincristine against chronic lymphocytic leukemia cells in vitro. Vilpo, J.A., Koski, T., Vilpo, L.M. Eur. J. Haematol. (2000) [Pubmed]
  28. Modulation of tubulin mRNA levels by interferon in human lymphoblastoid cells. Fellous, A., Ginzburg, I., Littauer, U.Z. EMBO J. (1982) [Pubmed]
  29. Molecular structures of human argininosuccinate synthetase pseudogenes. Evolutionary and mechanistic implications. Freytag, S.O., Bock, H.G., Beaudet, A.L., O'Brien, W.E. J. Biol. Chem. (1984) [Pubmed]
  30. The t-complex polypeptide 1 complex is a chaperonin for tubulin and actin in vivo. Sternlicht, H., Farr, G.W., Sternlicht, M.L., Driscoll, J.K., Willison, K., Yaffe, M.B. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  31. Intact microtubules are required for rapid turnover of carboxyl-terminal tyrosine of alpha-tubulin in cell cultures. Thompson, W.C., Deanin, G.G., Gordon, M.W. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  32. Tubulin heterogeneity in the trypanosome Crithidia fasciculata. Russell, D.G., Miller, D., Gull, K. Mol. Cell. Biol. (1984) [Pubmed]
  33. Elevated levels of microtubule destabilizing factors in a Taxol-resistant/dependent A549 cell line with an alpha-tubulin mutation. Martello, L.A., Verdier-Pinard, P., Shen, H.J., He, L., Torres, K., Orr, G.A., Horwitz, S.B. Cancer Res. (2003) [Pubmed]
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