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[Cancer Research 57, 130-135, January 1, 1997]
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Raf-1/bcl-2 Phosphorylation: A Step from Microtubule Damage to Cell Death

Mikhail V. Blagosklonny, Paraskevi Giannakakou, Wafik S. El-Deiry, David G. I. Kingston, Paul I. Higgs, Len Neckers and Tito Fojo1

Howard Hughes Medical Institute and Cancer Center, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104 [M. V. B., W. S. E-D.], Medicine Branch; NIH National Cancer Institute, Bethesda, Maryland 20892 [P. G., T. F.]; Department of Chemistry, Virginia Polytechnic Institute and State University, Blacksburg, Virginia 24061 [D. G. I. K., P. I. H.]; and Clinical Pharmacology Branch, NIH, National Cancer Institute, Bethesda, Maryland 20892 [L. N.]

Recent studies have shown that paclitaxel leads to activation of Raf-1 kinase and have suggested that this activation is essential for bcl-2 phosphorylation and apoptosis. In the present study, we demonstrate that, in addition to paclitaxel, other agents that interact with tubulin and microtubules also induce Raf-1/bcl-2 phosphorylation, whereas DNA-damaging drugs, antimetabolites, and alkylating agents do not. Activation of Raf-1 kinase by paclitaxel is linked to tubulin polymerization; the effect is blunted in paclitaxel-resistant cells, the tubulin of which does not polymerize following the addition of paclitaxel. In contrast, vincristine and vinblastine, drugs to which the paclitaxel-resistant cells retain sensitivity were able to bring about Raf-1 phosphorylation. The requirement for disruption of microtubules in this signaling cascade was strengthened further using paclitaxel analogues by demonstrating a correlation between tubulin polymerization, Raf-1/bcl-2 phosphorylation, and cytotoxicity. Inhibition of RNA or protein synthesis prevents Raf-1 activation and bcl-2 phosphorylation, suggesting that an intermediate protein(s) acts upstream of Raf-1 in this microtubule damage-activating pathway. A model is proposed that envisions a pathway of Raf-1 activation and bcl-2 phosphorylation following disruption of microtubular architecture, serving a role similar to p53 induction following DNA damage.

1 To whom requests for reprints should be addressed, at Medicine Branch, NIH, National Cancer Institute, Building 10, Room 12N226, 9000 Rockville Pike, Bethesda, MD 20892.

Received 9/26/96. Accepted 10/30/96.




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All along the watchtower: on the regulation of apoptosis regulator