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Taxol-induced Apoptosis and Phosphorylation of Bcl-2 Protein Involves c-Raf-1 and Represents a Novel c-Raf-1 Signal Transduction Pathway

Clinical Pharmacology Branch [M. V. B., T. S., L. M. N.] and Medicine Branch [P. N., J. T.], National Cancer Institute, NIH, Bethesda, Maryland 20892

c-Raf-1 (Raf-1) is a central component of signal transduction pathways stimulated by various growth factors, protein kinase C, and other protein kinases. Raf-1 activation is thought to be initiated at the plasma membrane after its recruitment by Ras. Raf-1 activation is associated primarily with proliferation and cell survival, but it has also been implicated in apoptosis. Raf-1 has also been shown to form complexes with both R-Ras and Bcl-2, raising the possibility that this component of cellular Raf-1 plays a role in apoptosis. Recently, taxol was reported to induce Bcl-2 phosphorylation and inactivation. We have previously demonstrated Raf-1 activation following taxol in MCF7 cells. We now present evidence that taxol fails to stimulate either apoptosis or phosphorylation of Bcl-2 in the absence of Raf-1. Moreover, Raf-1 activation by taxol coincided with Bcl-2 phosphorylation, showing similar dose and time dependence. Thus, our data support a role for a distinct subcellular component of Raf-1, which is taxol but not phorbol myristate acetate sensitive, in mediating an apoptotic pathway involving Bcl-2.

¹ Present address: University of Pennsylvania School of Medicine, Department of Hematology and Oncology, 437 CRB, 415 Curia Boulevard, Philadelphia, PA 19104.

² To whom requests for reprints should be addressed, at Clinical Pharmacology Branch, National Cancer Institute, NIH, Building 10, 12N226, Bethesda, MD 20892.

Received 11/ 3/95. Accepted 3/ 4/96.

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