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Gene Review

TUBBP2  -  tubulin, beta pseudogene 2

Homo sapiens

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Disease relevance of TUBBP2


Psychiatry related information on TUBBP2


High impact information on TUBBP2

  • The regulation of the microtubule system includes transcription of different tubulin isotypes, folding of /¿-tubulin heterodimers, post-translation modification of tubulin, and nucleotide-based microtubule dynamics, as well as interaction with numerous microtubule-associated proteins that are themselves regulated [10].
  • Under overexpression conditions, very short microtubules, or tubulin oligomers, are stabilized on Golgi membranes [11].
  • One of the most intriguing aspects of mitosis is the ability of kinetochores to hold onto plus ends of microtubules that are actively gaining or losing tubulin subunits [12].
  • The molecular systems covered included membrane rafts, actin and tubulin cytoskeleton, polarized transcription, signaling, and cell-cell adhesion [13].
  • Our observations indicate that Tbce is critical for the maintenance of microtubules in mouse motor axons, and suggest that altered function of tubulin cofactors might be implicated in human motor neuron diseases [14].

Chemical compound and disease context of TUBBP2


Biological context of TUBBP2

  • The inhibition of microtubule formation was shown to be mediated by interference with the colchicine binding site of tubulin [20].
  • Polycistronic transcription in these organisms makes the chromosomal arrangement of tubulin genes important with respect to gene expression [21].
  • CONCLUSION: Alternating and monotypic tubulin arrays were found to be mutually exclusive through comparison of genome sequences [21].
  • The role of microtubules in platelet aggregation and secretion has been analyzed using platelets permeabilized with digitonin and monoclonal antibodies to alpha (DM1A) and beta (DM1B) subunits of tubulin [22].
  • In TTL-null fibroblasts, tubulin detyrosination and CAP-Gly protein mislocalization correlate with defects in both spindle positioning during mitosis and cell morphology during interphase [23].

Anatomical context of TUBBP2

  • [4-(Imidazol-1-yl)thiazol-2-yl]phenylamines. A Novel Class of Highly Potent Colchicine Site Binding Tubulin Inhibitors: Synthesis and Cytotoxic Activity on Selected Human Cancer Cell Lines [20].
  • We aimed thus to study the effects of different tubulin ligands on the changes in the microtubule network and in several markers of cell injury and oxidative activity in cardiac muscle cells submitted to a reversible substrate-free, hypoxia-reoxygenation model of ischemia-reperfusion [24].
  • In cells of neural and non-neural origin, tubulin forms a complex with plasma membrane Na(+),K(+)-ATPase, resulting in inhibition of the enzyme activity [25].
  • Now, we found that in CAD cells, ATPase is not activated by L-glutamate and tubulin/ATPase complex is not present in membranes [25].
  • Using NAP affinity column and extracts from newborn rat brain (cerebral cortex), we now show that the above-mentioned peptides compete with NAP binding to tubulin [26].

Associations of TUBBP2 with chemical compounds

  • Neither compound seemed to induce an aberrant tubulin assembly reaction, as occurs with vinblastine (tight spirals) or dolastatin 10 (aggregated rings and spirals) [27].
  • Comparison of the Activities of the Truncated Halichondrin B Analog NSC 707389 (E7389) with Those of the Parent Compound and a Proposed Binding Site on Tubulin [27].
  • Inhibition of actin or tubulin polymerization, by using cytochalasin B or nocodazole, respectively, altered OP morphology and markedly impaired migration [28].
  • Tubulin-associated drug targets: Aurora kinases, Polo-like kinases, and others [29].
  • Cytosolic tubulin from trichostatin A-treated but not from non-treated cells inhibited ATPase activity [25].

Physical interactions of TUBBP2


Regulatory relationships of TUBBP2

  • Bulky substitution at position 11 determined different patterns of top2 cleavage sites and suppressed the action on tubulin [32].
  • COBRA-1 inhibited GTP-induced tubulin polymerization in cell-free tubulin turbidity assays [33].

Other interactions of TUBBP2


Analytical, diagnostic and therapeutic context of TUBBP2


  1. Radioimmunoassay for tubulin: a quantitative comparison of the tubulin content of different established tissue culture cells and tissues. Hiller, G., Weber, K. Cell (1978) [Pubmed]
  2. Microtubules in prokaryotes. Margulis, L., To, L., Chase, D. Science (1978) [Pubmed]
  3. Experimental phenylketonuria: replacement of carboxyl terminal tyrosine by phenylalanine in infant rat brain tubulin. Rodriguez, J.A., Borisy, G.G. Science (1979) [Pubmed]
  4. Studies in normal and chronic granulomatous disease neutrophils indicate a correlation of tubulin tyrosinolation with the cellular redox state. Nath, J., Gallin, J.I. J. Clin. Invest. (1983) [Pubmed]
  5. 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]
  6. Increased apoptosis in rat brain after rapid eye movement sleep loss. Biswas, S., Mishra, P., Mallick, B.N. Neuroscience (2006) [Pubmed]
  7. Diminished taxol/GTP-stimulated tubulin polymerization in diseased region of brain from patients with late-onset or inherited Alzheimer's disease or frontotemporal dementia with parkinsonism linked to chromosome-17 but not individuals with mild cognitive impairment. Boutté, A.M., Neely, M.D., Bird, T.D., Montine, K.S., Montine, T.J. J. Alzheimers Dis. (2005) [Pubmed]
  8. Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation. Dompierre, J.P., Godin, J.D., Charrin, B.C., Cordelières, F.P., King, S.J., Humbert, S., Saudou, F. J. Neurosci. (2007) [Pubmed]
  9. A highly epothilone B-resistant A549 cell line with mutations in tubulin that confer drug dependence. Yang, C.P., Verdier-Pinard, P., Wang, F., Lippaine-Horvath, E., He, L., Li, D., Höfle, G., Ojima, I., Orr, G.A., Horwitz, S.B. Mol. Cancer Ther. (2005) [Pubmed]
  10. Structural insights into microtubule function. Nogales, E. Annu. Rev. Biochem. (2000) [Pubmed]
  11. GMAP-210 recruits gamma-tubulin complexes to cis-Golgi membranes and is required for Golgi ribbon formation. Ríos, R.M., Sanchís, A., Tassin, A.M., Fedriani, C., Bornens, M. Cell (2004) [Pubmed]
  12. Human CLASP1 is an outer kinetochore component that regulates spindle microtubule dynamics. Maiato, H., Fairley, E.A., Rieder, C.L., Swedlow, J.R., Sunkel, C.E., Earnshaw, W.C. Cell (2003) [Pubmed]
  13. Shmoos, rafts, and uropods- the many facets of cell polarity. Dustin, M.L. Cell (2002) [Pubmed]
  14. A missense mutation in Tbce causes progressive motor neuronopathy in mice. Martin, N., Jaubert, J., Gounon, P., Salido, E., Haase, G., Szatanik, M., Guénet, J.L. Nat. Genet. (2002) [Pubmed]
  15. A common pharmacophore for epothilone and taxanes: molecular basis for drug resistance conferred by tubulin mutations in human cancer cells. Giannakakou, P., Gussio, R., Nogales, E., Downing, K.H., Zaharevitz, D., Bollbuck, B., Poy, G., Sackett, D., Nicolaou, K.C., Fojo, T. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  16. Phosphorylated tau can promote tubulin assembly. Tseng, H.C., Lu, Q., Henderson, E., Graves, D.J. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  17. Induction of apoptosis in proliferating human endothelial cells by the tumor-specific antiangiogenesis agent combretastatin A-4. Iyer, S., Chaplin, D.J., Rosenthal, D.S., Boulares, A.H., Li, L.Y., Smulson, M.E. Cancer Res. (1998) [Pubmed]
  18. Activities of the microtubule-stabilizing agents epothilones A and B with purified tubulin and in cells resistant to paclitaxel (Taxol(R)). Kowalski, R.J., Giannakakou, P., Hamel, E. J. Biol. Chem. (1997) [Pubmed]
  19. G beta gamma mediates the interplay between tubulin dimers and microtubules in the modulation of Gq signaling. Popova, J.S., Rasenick, M.M. J. Biol. Chem. (2003) [Pubmed]
  20. [4-(Imidazol-1-yl)thiazol-2-yl]phenylamines. A Novel Class of Highly Potent Colchicine Site Binding Tubulin Inhibitors: Synthesis and Cytotoxic Activity on Selected Human Cancer Cell Lines. Mahboobi, S., Sellmer, A., Höcher, H., Eichhorn, E., Bär, T., Schmidt, M., Maier, T., Stadlwieser, J.F., Beckers, T.L. J. Med. Chem. (2006) [Pubmed]
  21. Evolution of tubulin gene arrays in Trypanosomatid parasites: genomic restructuring in Leishmania. Jackson, A.P., Vaughan, S., Gull, K. BMC Genomics (2006) [Pubmed]
  22. The role of microtubules in platelet secretory release. Berry, S., Dawicki, D.D., Agarwal, K.C., Steiner, M. Biochim. Biophys. Acta (1989) [Pubmed]
  23. Tubulin tyrosination is a major factor affecting the recruitment of CAP-Gly proteins at microtubule plus ends. Peris, L., Thery, M., Fauré, J., Saoudi, Y., Lafanechère, L., Chilton, J.K., Gordon-Weeks, P., Galjart, N., Bornens, M., Wordeman, L., Wehland, J., Andrieux, A., Job, D. J. Cell Biol. (2006) [Pubmed]
  24. Tubulin ligands suggest a microtubule-NADPH oxidase relationship in postischemic cardiomyocytes. Devillard, L., Vandroux, D., Tissier, C., Brochot, A., Voisin, S., Rochette, L., Athias, P. Eur. J. Pharmacol. (2006) [Pubmed]
  25. Tubulin must be acetylated in order to form a complex with membrane Na(+),K (+)-ATPase and to inhibit its enzyme activity. Santander, V.S., Bisig, C.G., Purro, S.A., Casale, C.H., Arce, C.A., Barra, H.S. Mol. Cell. Biochem. (2006) [Pubmed]
  26. Tubulin is the target binding site for NAP-related peptides: ADNF-9, D-NAP, and D-SAL. Holtser-Cochav, M., Divinski, I., Gozes, I. J. Mol. Neurosci. (2006) [Pubmed]
  27. Comparison of the Activities of the Truncated Halichondrin B Analog NSC 707389 (E7389) with Those of the Parent Compound and a Proposed Binding Site on Tubulin. Dabydeen, D.A., Burnett, J.C., Bai, R., Verdier-Pinard, P., Hickford, S.J., Pettit, G.R., Blunt, J.W., Munro, M.H., Gussio, R., Hamel, E. Mol. Pharmacol. (2006) [Pubmed]
  28. Intracellular signals and cytoskeletal elements involved in oligodendrocyte progenitor migration. Simpson, P.B., Armstrong, R.C. Glia (1999) [Pubmed]
  29. Tubulin-associated drug targets: Aurora kinases, Polo-like kinases, and others. Warner, S.L., Gray, P.J., Von Hoff, D.D. Semin. Oncol. (2006) [Pubmed]
  30. Probing the native structure of stathmin and its interaction domains with tubulin. Combined use of limited proteolysis, size exclusion chromatography, and mass spectrometry. Redeker, V., Lachkar, S., Siavoshian, S., Charbaut, E., Rossier, J., Sobel, A., Curmi, P.A. J. Biol. Chem. (2000) [Pubmed]
  31. Localization of specific epitopes on human microtubule-associated protein 2. Kalcheva, N., Albala, J.S., Binder, L.I., Shafit-Zagardo, B. J. Neurochem. (1994) [Pubmed]
  32. Azatoxin derivatives with potent and selective action on topoisomerase II. Leteurtre, F., Sackett, D.L., Madalengoitia, J., Kohlhagen, G., MacDonald, T., Hamel, E., Paull, K.D., Pommier, Y. Biochem. Pharmacol. (1995) [Pubmed]
  33. COBRA-1, a rationally-designed epoxy-THF containing compound with potent tubulin depolymerizing activity as a novel anticancer agent. Jan, S.T., Mao, C., Vassilev, A.O., Navara, C.S., Uckun, F.M. Bioorg. Med. Chem. Lett. (2000) [Pubmed]
  34. p53 is associated with cellular microtubules and is transported to the nucleus by dynein. Giannakakou, P., Sackett, D.L., Ward, Y., Webster, K.R., Blagosklonny, M.V., Fojo, T. Nat. Cell Biol. (2000) [Pubmed]
  35. Serum antibodies against central nervous system proteins in human demyelinating disease. Newcombe, J., Gahan, S., Cuzner, M.L. Clin. Exp. Immunol. (1985) [Pubmed]
  36. Identification of a novel beta-tubulin subfamily with one member (TUBB4Q) located near the telomere of chromosome region 4q35. van Geel, M., van Deutekom, J.C., van Staalduinen, A., Lemmers, R.J., Dickson, M.C., Hofker, M.H., Padberg, G.W., Hewitt, J.E., de Jong, P.J., Frants, R.R. Cytogenet. Cell Genet. (2000) [Pubmed]
  37. HURP Wraps Microtubule Ends with an Additional Tubulin Sheet That Has a Novel Conformation of Tubulin. Santarella, R.A., Koffa, M.D., Tittmann, P., Gross, H., Hoenger, A. J. Mol. Biol. (2007) [Pubmed]
  38. Tubulin-binding drug screening by MALDI-TOFMS. Hannewald, P., Maunit, B., Muller, J.F. Anal. Chem. (2006) [Pubmed]
  39. Single microtubules from squid axoplasm support bidirectional movement of organelles. Schnapp, B.J., Vale, R.D., Sheetz, M.P., Reese, T.S. Cell (1985) [Pubmed]
  40. Phagokinetic tracks of 3T3 cells: parallels between the orientation of track segments and of cellular structures which contain actin or tubulin. Albrecht-Buehler, G. Cell (1977) [Pubmed]
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