Regulation of Bcl2 phosphorylation by stress response kinase pathway.

  • Authors:
    • A Basu
    • S A You
    • S Haldar
  • View Affiliations

  • Published online on: March 1, 2000     https://doi.org/10.3892/ijo.16.3.497
  • Pages: 497-997
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Abstract

The anticancer drugs affecting either microtubule polymerization or depolymerization could trigger Bcl2 phosphorylation in mitotic phase of the cell cycle. By systematic site directed mutagenesis studies, we have previously mapped taxol induced phosphorylation sites to be Ser-70 and 87 residues of Bcl2 protein. Interestingly, sequences surrounding both serine-70 and serine-87 residues represent MAP kinase consensus motif. Since Bcl2 phosphorylation predominantly occurs at site consensus to MAP kinase family members, we were interested to test whether Erk2 or Jun kinase is involved in this pathway. Our in vitro studies document that stress activated kinase, JNK1 is responsible for Bcl2 phosphorylation.

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March 2000
Volume 16 Issue 3

Print ISSN: 1019-6439
Online ISSN:1791-2423

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APA
Basu, A., You, S., & Haldar, S. (2000). Regulation of Bcl2 phosphorylation by stress response kinase pathway.. International Journal of Oncology, 16, 497-997. https://doi.org/10.3892/ijo.16.3.497
MLA
Basu, A., You, S., Haldar, S."Regulation of Bcl2 phosphorylation by stress response kinase pathway.". International Journal of Oncology 16.3 (2000): 497-997.
Chicago
Basu, A., You, S., Haldar, S."Regulation of Bcl2 phosphorylation by stress response kinase pathway.". International Journal of Oncology 16, no. 3 (2000): 497-997. https://doi.org/10.3892/ijo.16.3.497