Differential expression of tubulin isotypes during the cell cycle

Dumontet, Charles; Durán, George E.; Steger, Katherine A.; Murphy, Gloria A.; Sussman, Howard H.; Šikić, Branimir I.

doi:10.1002/(sici)1097-0169(1996)35:1<49::aid-cm4>3.0.co;2-d

Cited by 32 publications

(26 citation statements)

References 38 publications

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“…4, ␥-tubulin mRNA levels remain relatively unchanged during either HU treatment (when centrosomes are overproduced) or when Stat3 is inhibited (and centrosome production is blocked). Along with previous results, which demonstrate that ␥-tubulin levels do not fluctuate during the cell cycle (37), the data indicate that ␥-tubulin behaves more like a housekeeping gene, in that its mRNA production does not depend on growth factor activation or cell cycling. However, it is difficult to explain the precipitous drop in ␥-tubulin protein levels when Stat3 activity is blocked.…”

Section: Discussionsupporting

confidence: 86%

Stat3 Activity Is Required for Centrosome Duplication in Chinese Hamster Ovary Cells

Metge¹,

Ofori-Acquah

Stevens

et al. 2004

Journal of Biological Chemistry

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Section: Discussionsupporting

confidence: 86%

Stat3 Activity Is Required for Centrosome Duplication in Chinese Hamster Ovary Cells

Metge¹,

Ofori-Acquah

Stevens

et al. 2004

Journal of Biological Chemistry

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“…Tubulin immunodection (Fig. 3B, tubulin) used to verify protein loading showed the expected pattern of constitutive levels across the times examined (Dumontet et al, 1996). Taken together, the results from Figs 1, 2 and 3 show that the binding activity of YY1 dramatically increases at the G1/S boundary but that this increase in activity is not reflected in changes in the levels of mRNA or protein abundance over the same time intervals.…”

Section: Resultsmentioning

confidence: 56%

The Yin Yang-1 (YY1) protein undergoes a DNA-replication-associated switch in localization from the cytoplasm to the nucleus at the onset of S phase

Palko

Bass

Beyrouthy

et al. 2004

Journal of Cell Science

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The essential Yin Yang-1 gene (YY1) encodes a ubiquitous, conserved, multifunctional zinc-finger transcription factor in animals. The YY1 protein regulates initiation, activation, or repression of transcription from a variety of genes required for cell growth, development, differentiation, or tumor suppression, as well as from genes in some retroviruses and DNA viruses. Among the specific functions attributed to YY1 is a role in cell-cycle-specific upregulation of the replication-dependent histone genes. The YY1 protein binds to the histone alpha element, a regulatory sequence found in all replication-dependent histone genes. We therefore examined the abundance, DNA-binding activity and localization of the YY1 protein throughout the cell cycle in unperturbed, shake-off-synchronized Chinese hamster ovary and HeLa cells. We found that, whereas the DNA-binding activity of YY1 increased dramatically early in S phase, the YY1 mRNA and protein levels did not. YY1 changed subcellular distribution patterns during the cell cycle, from mainly cytoplasmic at G1 to mainly nuclear at early and middle S phase, then back to primarily cytoplasmic later in S phase. Nuclear accumulation of YY1 near the G1/S boundary coincided with both an increase in YY1 DNA-binding activity and the coordinate up-regulation of the replication-dependent histone genes. The DNA synthesis inhibitor aphidicolin caused a nearly complete loss of nuclear YY1, whereas addition of caffeine or 2-aminopurine to aphidicolin-treated cells restored both DNA synthesis and YY1 localization in the nucleus. These findings reveal a mechanism by which YY1 localization is coupled to DNA synthesis and responsive to cell-cycle signaling pathways. Taken together, our results provide insight into how YY1 might participate in the cell-cycle control over a variety of nuclear events required for cell division and proliferation.

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“…Cell cycle analysis of h-tubulin isotype expression has previously been examined in leukemic and sarcoma cell lines (35). Both hIVa-and hIVb-tubulin gene levels were found to be expressed at twice the levels in dividing cells than in resting cells.…”

Section: Discussionmentioning

confidence: 99%

Tubulin-Targeted Drug Action: Functional Significance of Class II and Class IVb β-Tubulin in Vinca Alkaloid Sensitivity

Gan

Kavallaris

2008

Cancer Research

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Aberrant expression of B-tubulin isotypes is frequently described in tumor tissues and tubulin-binding agent (TBA)-resistant cell lines. There is limited understanding of the role of specific B-tubulin isotypes in cellular sensitivity to TBAs, and to gain insights into the functional role of BII-and BIVb-tubulin, we examined these isotypes in lung cancer cell lines NCI-H460 (H460) and Calu-6. Drug-treated clonogenic assays revealed that small interfering RNA-mediated knockdown of either BII-or BIVb-tubulin hypersensitized the lung cancer cell lines to Vinca alkaloids, with the effects more pronounced following BIVb-tubulin knockdown. In contrast, there was no change in paclitaxel sensitivity following knockdown of either isotype. Cell cycle analysis revealed a greater propensity for the BII-and BIVb-tubulin knockdown cells to undergo G 2 -M cell cycle block following 5 nmol/L vincristine treatment, with the BIVb knockdown cells being more sensitive than the BII-tubulin knockdown cells compared with control. In contrast to BII-tubulin knockdown, BIVb-tubulin knockdown cells showed a significant increase in the sub-G 1 population (cell death) following treatment with both 5 and 40 nmol/L of vincristine compared with controls. Importantly, BIVb-tubulin knockdown in H460 cells caused a significant dose-dependent increase in Annexin V staining in response to vincristine but not paclitaxel. Therefore, increased sensitivity to induction of apoptosis is one mechanism underlying the Vinca alkaloid hypersensitivity. This study provides direct evidence that BII-or BIVb-tubulins have functionally distinct roles and expression of these isotypes may serve as strong predictors of Vinca alkaloid response and resistance. [Cancer Res 2008;68(23):9817-24]

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Differential expression of tubulin isotypes during the cell cycle

Cited by 32 publications

References 38 publications

Stat3 Activity Is Required for Centrosome Duplication in Chinese Hamster Ovary Cells

Stat3 Activity Is Required for Centrosome Duplication in Chinese Hamster Ovary Cells

The Yin Yang-1 (YY1) protein undergoes a DNA-replication-associated switch in localization from the cytoplasm to the nucleus at the onset of S phase

Tubulin-Targeted Drug Action: Functional Significance of Class II and Class IVb β-Tubulin in Vinca Alkaloid Sensitivity

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