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* The Beatson Institute for Cancer Research, Garscube Estate, Glasgow G61 1BD, U.K.;
GSF-Forschungszentrum für Umwelt und Gesundheit, Institut für Klinische Molekularbiologie und Tumorgenetik, D-81377 München, Germany;
Institute De Biochimie, Universite Lausanne, CH 1066 Epalinges, Switzerland;
§ Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA;
¶ The Salk Institute, La Jolla, California 92037, USA;
Institute of Microbiology and Genetics, Vienna Biocenter, A-1030 Vienna, Austria; and
Department of Nephrology, Medizinische Hochschule Hannover, 30625 Hannover, Germany
1Correspondence: The Beatson Institute for Cancer Research, Garscube Estate, Switchback Road, Bearsden, Glasgow G61 1BD, U.K. E-mail: pjanosch{at}beatson.gla.ac.uk
Using immobilized GST-Raf-1 as bait, we have isolated the intermediate filament protein vimentin as a Raf-1-associated protein. Vimentin coimmunoprecipitated and colocalized with Raf-1 in fibroblasts. Vimentin was not a Raf-1 substrate, but was phosphorylated by Raf-1-associated vimentin kinases. We provide evidence for at least two Raf-1-associated vimentin kinases and identified one as casein kinase 2. They are regulated by Raf-1, since the activation status of Raf-1 correlated with the phosphorylation of vimentin. Vimentin phosphorylation by Raf-1 preparations interfered with its polymerization in vitro. A subset of tryptic vimentin phosphopeptides induced by Raf-1 in vitro matched the vimentin phosphopeptides isolated from v-raf-transfected cells labeled with orthophosphoric acid, indicating that Raf-1 also induces vimentin phosphorylation in intact cells. In NIH 3T3 fibroblasts, the selective activation of an estrogen-regulated Raf-1 mutant induced a rearrangement and depolymerization of the reticular vimentin scaffold similar to the changes elicited by serum treatment. The rearrangement of the vimentin network occurred independently of the MEK/ERK pathway. These data identify a new branch point in Raf-1 signaling, which links Raf-1 to changes in the cytoskeletal architecture.—Janosch, P., Kieser, A., Eulitz, M., Lovric, J., Sauer, G., Reichert, M., Gounari, F., Büscher, D., Baccarini, M., Mischak, H., Kolch, W. The Raf-1 kinase associates with vimentin kinases and regulates the structure of vimentin filaments.
Key Words: Raf • phosphorylation • cytoskeleton • casein kinase 2
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