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Originally published In Press as doi:10.1074/jbc.M404440200 on August 19, 2004

J. Biol. Chem., Vol. 279, Issue 46, 48319-48328, November 12, 2004
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The Oncogenic Serine/Threonine Kinase Pim-1 Phosphorylates and Inhibits the Activity of Cdc25C-associated Kinase 1 (C-TAK1)

A NOVEL ROLE FOR Pim-1 AT THE G2/M CELL CYCLE CHECKPOINT*

Malte Bachmann{ddagger}§, Hanjo Hennemann{ddagger}, Pei Xiang Xing||, Ingrid Hoffmann**, and Tarik Möröy{ddagger}{ddagger}{ddagger}

From the {ddagger}Institut für Zellbiologie (Tumorforschung), IFZ, Universitätsklinikum Essen, Virchowstrasse 173, D-45122 Essen, Germany, the ||Austin Research Institute, Cancer Immunotherapy Laboratory, Heidelberg, Victoria 3084, Australia, and the **Deutsches Krebsforschungszentrum, DKFZ, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany

The Pim-1 oncogene encodes a serine-threonine kinase that relays signals from cytokine receptors and contributes to the formation of lymphoid tumors when expressed at high levels. Here we show that the protein kinase Cdc25 C-associated kinase 1 (C-TAK1) is a binding partner and a substrate of Pim-1. A physical interaction of Pim-1 and C-TAK1 could be shown biochemically and in yeast two-hybrid assays. Immunofluorescence experiments suggested that Pim-1·C-TAK1 complexes are predominantly cytoplasmic. When transiently transfected, Pim-1 was also found in the nucleus and could recruit C-TAK1 to this compartment. Both Pim-1 and C-TAK1 underwent autophosphorylation, but only Pim-1 was able to phosphorylate C-TAK1 but not vice versa. Mass spectrometry analysis of C-TAK1 suggested that the sites of autophosphorylation and Pim-1-mediated phosphorylation are distinct and not overlapping. Phosphorylation by Pim-1 decreased C-TAK1 kinase activity significantly, in particular its ability to phosphorylate and inactivate Cdc25C, a protein that actively promotes cell cycle progression at the G2/M phase. Hence our findings directly suggest a novel role for Pim-1 as a positive regulator at the G2/M transition of the cell cycle.

Received for publication, April 22, 2004 , and in revised form, August 19, 2004.

* This work was supported by Grant Mo 435–16/1, 16/2 from the Deutsche Forschungsgemeinschaft, DFG and the Fonds der Chemischen Industrie. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: pharmazentrum frankfurt, Universitätsklinikum, Theodor Stern kai 7, D-60590 Frankfurt/Main, Germany.

Present address: Caesar, Centre of Advanced European Studies and Research, Ludwig-Erhard-Allee 2, D-53175 Bonn, Germany.

{ddagger}{ddagger} To whom correspondence should be addressed: Institut für Zellbiologie (Tumorforschung), IFZ, Virchowstrasse 173, D-45122 Essen, Germany. Tel.: 49-201-723-3380; Fax: 49-201-723-5904; E-mail: moeroey{at}uni-essen.de.


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