Identification of Two Human β-Tubulin Isotypes

Hall, J. L.; Dudley, L; Dobner, Paul R.; Lewis, Sally A.; Cowan, Nicholas J.

doi:10.1128/mcb.3.5.854-862.1983

Cited by 6 publications

(2 citation statements)

References 42 publications

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“…The pRI clone was kindly provided by S. McKnight. The same filter was washed free of probe and rehybridized with a 0.8-kilobase (kb) PstI fragment of a cDNA human ,-tubulin cDNA clone (14). (C. Whitfield provided the 1-tubulin clone, which was isolated in the laboratory of N.…”

Section: Methodsmentioning

confidence: 99%

Cyclic AMP-Dependent Protein Kinase Regulates Sensitivity of Cells to Multiple Drugs

Abraham

Hunter

Sampson

et al. 1987

Molecular and Cellular Biology

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The isolation of mutant cell lines affecting the activity of cyclic AMP (cAMP)-dependent protein kinase (PK-A) has made it possible to determine the function of this kinase in mammalian cells. We found that both a CHO cell mutant with a defective regulatory subunit (RI) for PK-A and a transfectant cell line expressing the same mutant kinase were sensitive to multiple drugs, including puromycin, adriamycin, actinomycin D, and some antimitotic drugs. The mutant and transfectant cells, after treatment with a concentration of the antimitotic drug colcemid that had no marked effect on the wild-type parent cell, had a severely disrupted microtubule network. The phenotype of hypersensitivity to the antimitotic drug colcemid was used to select revertants of the transfectant and the original mutant. These revertants simultaneously regained normal multiple drug resistance and cAMP sensitivity, thus establishing that the characteristics of colcemid sensitivity and cAMP resistance are linked. Four revertants of the transfectant reverted because of loss or rearrangement of the transfected mutant RI gene. These revertants, as well as one revertant selected from the original mutant, had PK-A activities equal to or higher than that of the parent. In these genetic studies, in which linkage of expression of a PK-A mutation with drug sensitivity is demonstrated, it was established that the PK-A system is involved in regulating resistance of mammalian cells to multiple drugs.

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Section: Methodsmentioning

confidence: 99%

Cyclic AMP-Dependent Protein Kinase Regulates Sensitivity of Cells to Multiple Drugs

Abraham

Hunter

Sampson

et al. 1987

Molecular and Cellular Biology

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“…This initial alignment was then filtered for both duplicate and fragmentary sequences, producing a final set of 23 unique sequences. Based upon differences found in each protein's carboxyterminal tail region, ten consensus sequences corresponding to tubulin isotypes βI, βIIa/b, βIII, βIVa/b, βV, βVI, βVII and βVIII, were characterized (figure 1) [36][37][38][39][40]. Of these Sequence alignment of β tubulin isotypes.…”

Section: Modelling Human β Tubulin Isotypesmentioning

confidence: 99%

Comparative modelling of human β tubulin isotypes and implications for drug binding

2006

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The protein tubulin is a target for several anti-mitotic drugs, which affect microtubule dynamics, ultimately leading to cell cycle arrest and apoptosis. Many of these drugs, including the taxanes and Vinca alkaloids, are currently used clinically in the treatment of several types of cancer. Another tubulin binding drug, colchicine, although too toxic to be used as a chemotherapeutic agent, is commonly used for the treatment of gout. The main disadvantage that all of these drugs share is that they bind tubulin indiscriminately, leading to the death of both cancerous and healthy cells. However, the broad cellular distribution of several tubulin isotypes provides a platform upon which to construct novel chemotherapeutic drugs that could differentiate between different cell types, reducing the undesirable side effects associated with current chemotherapeutic treatments. Here, we report an analysis of ten human β tubulin isotypes and discuss differences within each of the previously characterized paclitaxel, colchicine and vinblastine binding sites.

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A Codon Change in β-Tubulin Which Drastically Affects Microtubule Structure in Drosophila melanogaster Fails To Produce a Significant Phenotype in Saccharomyces cerevisiae

Praitis

Katz

Solomon

1991

Molecular and Cellular Biology

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The relative uniformity of microtubule ultrastructure in almost all eukaryotic cells is thought to be a consequence of the conserved elements of tubulin sequence. In support of this idea, a mutation in a beta-tubulin gene of Drosophila melanogaster, occurring at a highly conserved position, produces U-shaped microtubules, suggesting a defect in either nucleation or packing during assembly (M. T. Fuller, J. H. Caulton, J. A. Hutchens, T. C. Kaufman, and E. C. Raff, J. Cell Biol. 104:385-394, 1987, and J. E. Rudolph, M. Kimble, H. D. Hoyle, M. A. Subler, and E. C. Raff, Mol. Cell. Biol. 7:2231-2242, 1987). Surprisingly, we find that introducing the same mutation into the sole beta-tubulin gene of Saccharomyces cerevisiae has virtually no consequences for microtubule structure or function in that organism.

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Identification of Two Human β-Tubulin Isotypes

Cited by 6 publications

References 42 publications

Cyclic AMP-Dependent Protein Kinase Regulates Sensitivity of Cells to Multiple Drugs

Cyclic AMP-Dependent Protein Kinase Regulates Sensitivity of Cells to Multiple Drugs

Comparative modelling of human β tubulin isotypes and implications for drug binding

A Codon Change in β-Tubulin Which Drastically Affects Microtubule Structure in Drosophila melanogaster Fails To Produce a Significant Phenotype in Saccharomyces cerevisiae

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