Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1

Hong Gang Wang, Shinichi Takayama, Ulf R. Rapp, John C. Reed

Research output: Contribution to journalArticlepeer-review

325 Scopus citations

Abstract

The Bcl-2 protein blocks programmed cell death (apoptosis) through an unknown mechanism. Previously we identified a Bcl-2 interacting protein BAG-1 that enhances the anti-apoptotic effects of Bcl-2. Like BAG-1, the serine/threonine protein kinase Raf-1 also can functionally cooperate with Bcl-2 in suppressing apoptosis. Here we show that Raf-1 and BAG-1 specifically interact in vitro and in yeast two-hybrid assays. Raf-1 and BAG-1 can also be coimmunoprecipitated from mammalian cells and from insect cells infected with recombinant baculoviruses encoding these proteins. Furthermore, bacterially-produced BAG-1 protein can increase the kinase activity of Raf-1 in vitro. BAG-1 also activates this mammalian kinase in yeast. These observations suggest that the Bcl-2 binding protein BAG-1 joins Ras and 14-3-3 proteins as potential activators of the kinase Raf-1.

Original languageEnglish (US)
Pages (from-to)7063-7068
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume93
Issue number14
DOIs
StatePublished - Jul 9 1996

All Science Journal Classification (ASJC) codes

  • General

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