Disease relevance of TUBA1B

• In the present work insulin was found to rapidly, but transiently, increase transcription of the cytoskeletal beta-actin and alpha-tubulin genes in rat H4IIE hepatoma cells [1].
• Expression of beta-actin and alpha-tubulin mRNA in gerbil brain following transient ischemia and reperfusion up to 1 month [2].
• In addition to showing tumor growth inhibition, we identified three potential surrogate biomarkers to determine the efficacy of 2-methoxyestradiol therapy: decreased HIF-1alpha levels, alpha-tubulin acetylation, and degree of hypoxia as determined by pimonidazole staining [3].
• In contrast, alpha-tubulin expressed in E. coli lysates was incapable of coassemblying with bovine brain tubulin [4].
• Normal and prostate cancer cells display distinct molecular profiles of alpha-tubulin posttranslational modifications [5].

Psychiatry related information on TUBA1B

• Reduction of acetylated alpha-tubulin immunoreactivity in neurofibrillary tangle-bearing neurons in Alzheimer's disease [6].
• Accordingly, the present paper investigated the effects of social isolation on hippocampal levels of alpha-tubulin isoforms associated with microtubule dynamics, the dendritic marker MAP-2 and alterations in locomotor activity and recognition memory [7].

High impact information on TUBA1B

• Our findings provide a molecular basis for understanding the modular interaction modes between alpha-tubulin, CLIPs, EB proteins, and the dynactin-dynein motor complex and suggest that multiple low-affinity binding sites in different combinations control dynamic +TIP networks at microtubule ends [8].
• SIRT2 deacetylates lysine-40 of alpha-tubulin both in vitro and in vivo [9].
• The centrosome organizes microtubules, which are made up of alpha-tubulin and beta-tubulin, and contains centrosome-bound gamma-tubulin, which is involved in microtubule nucleation [10].
• Tubulin from both normal and Alzheimer brains was labelled on western blots by a monoclonal antibody to the tyrosinylated carboxy-terminal epitope of alpha tubulin [11].
• Near-simultaneous three-dimensional fluorescence/differential interference contrast microscopy was used to follow the behavior of microtubules and chromosomes in living alpha-tubulin/GFP-expressing cells after inhibition of the mitotic kinesin Eg5 with monastrol [12].

Biological context of TUBA1B

• To examine the sequence complexity and differential expression of human alpha-tubulin genes, we constructed cDNA libraries from two unrelated tissue types (epidermis and fetal brain) [13].
• This property has been used to dissect the human alpha-tubulin multigene family into members bearing sequence relatedness in this region [13].
• Using mutagenesis, we provide evidence that beta-actin and alpha-tubulin each have two prefoldin interaction sites [14].
• Mock transfections had no effect on HSMC contractily, and transfections with small interfering RNAs (siRNAs) specific for HDAC6, a cytosolic HDAC that functions as an alpha-tubulin deacetylase, resulted in a weak contraction inhibition [15].
• Site-directed mutagenesis of alpha-tubulin. Reductive methylation studies of the Lys 394 region [16].

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

• Lys 394 in a human keratinocyte alpha-tubulin (k alpha 1) was replaced by a glutamic acid residue using site-directed mutagenesis [16].
• Inclusion of 3-nitro-l-tyrosine (NO(2)Tyr) in the culture medium resulted in the selective nitrotyrosination of alpha-tubulin, that was paralleled by decreased elaboration of Glu-tubulin, decreased expression of cyclins A and E, decreased association of the microtubule plus-end binding protein EB1, and inhibited cell proliferation [21].
• In addition to the specific microtubule frameworks already mentioned, cytoplasmic microtubules resistant to nocodazole or colchicine, but not cold-resistant microtubules, contain more acetylated alpha-tubulin than the rest of cellular microtubules [22].
• Genes for alpha-tubulin, beta-tubulin and elongation factor 1 alpha (EF-1alpha) from two unclassified strains of Hexamitidae were found to contain TAA and TAG (TAR) triplets at positions suggesting a variant code in which TAR codes for glutamine [23].
• Treatment of this pellet with KI released NPA binding activity, actin, and alpha-tubulin [24].

Regulatory relationships of TUBA1B

• In metaphase, annexin XI was up-regulated and costained with alpha-tubulin [25].

Other interactions of TUBA1B

• HPRT1, ALAS1, and K-ALPHA-1 were calculated by both programs to be the most stable genes covering a broad range of expression [26].
• Immunostaining of filamentous structures of CLL cells revealed that vincristine brings about selective changes in alpha-tubulin but not in beta-actin or vimentin [27].
• In situ hybridization revealed a decline in the mRNA expressions of both alpha-tubulin and beta-actin in the CA1 region as early as 6-24 h PI with the reductions being prominent at 3 days PI [2].
• Two-dimensional gel electrophoresis of the labeled protein products directed by mRNA indicates that IFN caused a more pronounced increase in the level of alpha-tubulin than beta-tubulin mRNA [28].
• These data indicate that the expressed argininosuccinate synthetase gene is evolving at a rate similar to that of the beta-globin gene and much faster than the alpha-tubulin gene [29].

Analytical, diagnostic and therapeutic context of TUBA1B

• When extracts of pulse-labeled cells were analyzed by anion-exchange and size-exclusion chromatography, newly synthesized alpha-tubulin, beta-tubulin, and actin were observed to enter a large molecular mass complex (approximately 900 kDa) [30].
• The time course of mRNA expressions of two cytoskeletal proteins, beta-actin and alpha-tubulin, was studied by Northern blot analysis and in situ hybridization in the same gerbil brains at various periods of recirculation following 10 min of forebrain ischemia [2].
• Intact microtubules are required for rapid turnover of carboxyl-terminal tyrosine of alpha-tubulin in cell cultures [31].
• Peptide mapping data indicated that cytoplasmic alpha tubulin is the most likely precursor [32].
• The expression of the alpha-tubulin mutation was demonstrated using high-resolution isoelectric focusing and two-dimensional gel analysis [33].

References