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J. Biol. Chem., Vol. 281, Issue 22, 15138-15144, June 2, 2006

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CUTL1 Is Phosphorylated by Protein Kinase A, Modulating Its Effects on Cell Proliferation and Motility^*

Patrick Michl, Beate Knobel, and Julian Downward¹

From the Signal Transduction Laboratory, Cancer Research UK London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, United Kingdom and Universitätsklinikum Ulm, Abteilung Innere Medizin I, Robert-Koch-Strasse 8, 89081 Ulm, Germany

CUTL1, also known as CDP (CCAAT Displacement Protein), Cut, or Cux-1, is a homeodomain transcription factor known to play an essential role in development and cell cycle progression. Previously, we identified CUTL1 as modulator of cell motility and invasiveness. Here we report that protein kinase A (PKA), known to inhibit tumor progression in various tumor types, directly phosphorylates CUTL1 at serine 1215 in NIH3T3 fibroblasts. The PKA-induced phosphorylation results in decreased DNA binding affinity of CUTL1 and diminished CUTL1-mediated cell cycle progression and cell motility. Furthermore, the expression of several CUTL1 target genes involved in proliferation and migration, such as DNA polymerase A and DKK2, was modulated by PKA-induced phosphorylation. These data identify CUTL1 as a novel target of PKA through which this protein kinase can modulate tumor cell motility and tumor progression.

Received for publication, January 30, 2006 , and in revised form, March 29, 2006.

^* This work was supported in part by a research fellowship from the Deutsche Forschungsgemeinschaft (to P. M.) and by Cancer Research UK. 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.

¹ To whom correspondence should be addressed. Tel.: 44-20-7269-3533; Fax: 44-20-7269-3094; E-mail: downward{at}cancer.org.uk.

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