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Interaction between the Protein Kinase B-Raf and the -Subunit of the 11S Proteasome Regulator¹

Institut für Medizinische Strahlenkunde und Zellforschung (MSZ), University of Würzburg, 97078 Würzburg, Germany [C. H., C. K. W., L. W., T. S., U. R. R.], and Department of Surgery, University of Washington, Seattle, Washington 98195 [A. K.]

Protein kinases of the Raf family act as signal-transducing elements downstream of activated cell surface receptors and are involved in the regulation of proliferation, differentiation, and cell survival. Whereas the role of c-Raf-1 as a mitogen-activated protein/extracellular signal-regulated kinase activator within the mitogenic cascade is well established, less is known about the mammalian Raf isoforms A-Raf and B-Raf. Here we report that B-Raf binds to PA28, one of two subunits of the 11S regulator of proteasomes. PA28 was isolated as a B-Raf-binding protein in a yeast two-hybrid screen of a PC12 cDNA library. Both proteins can be coimmunoprecipitated after transient expression in 293 cells. No association could be found between PA28 and A-Raf or c-Raf-1. B-Raf binds to a region in PA28 that is important for its proteasome-activating function.

¹ Supported by Grants RA642/1-1, WE2023/2-1, and SFB 172 from the Deutsche Forschungsgemeinschaft.

² A. K. and C. H. contributed equally to this work.

³ To whom requests for reprints should be addressed, at Institut für Medizinische Strahlenkunde und Zellforschung (MSZ), University of Würzburg, Versbacher Strasse 5, 97078 Würzburg, Germany. Phone: 49-931-201-5140; Fax: 49-931-201-3835.

Received 5/14/98. Accepted 5/29/98.

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