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• W2340245588 startingPage "75" @default.
• W2340245588 abstract "It has been widely accepted that the oncogene product bcl-2 protects mammalian cells from programmed cell death (apoptosis). The molecules and signalling pathways upon which bcl-2 acts are, however, still ill-defined. Recently, bcl-2 was shown to interact with c-raf-1 in vitro. Furthermore, an active form of c-raf-1 delayed apoptosis induced by trophic factor deprivation and enhanced the death-suppressive function of bcl-2 when co-expressed. This has led to the hypothesis that bcl-2 communicates cell-death protection via a raf-dependent signal transduction pathway. Here we show, by various immunological and biochemical methods, that bcl-2 does not stably associate with c-raf-1 in cellular extracts prepared from fibroblasts before or after treatment with agents that induce apoptosis. Unexpectedly, bcl-2 function is entirely maintained, if not improved, when raf-dependent signalling is experimentally abrogated. In fact, bcl-2 allows the stable overexpression of a kinase-defective dominant-negative raf mutant that usually interferes with cell viability and/or proliferation. Our results indicate that bcl-2 does not require c-raf-1 kinase activity and an associated mitogen-activated protein kinase signalling pathway for its survival function. This property may be exploited to dissect cellular events that are dependent or independent of c-raf-1 kinase activity." @default.
• W2340245588 created "2016-06-24" @default.
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• W2340245588 date "1997-05-15" @default.
• W2340245588 modified "2023-10-11" @default.
• W2340245588 title "Bcl-2 does not require Raf kinase activity for its death-protective function" @default.
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• W2340245588 doi "https://doi.org/10.1042/bj3240075" @default.
• W2340245588 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1218403" @default.
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• W2340245588 hasPublicationYear "1997" @default.
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