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Science 9 May 1997:
Vol. 276. no. 5314, pp. 952 - 955
DOI: 10.1126/science.276.5314.952
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Reports

Regulation of Protein Phosphatase 2A by Direct Interaction with Casein Kinase 2alpha

Jean-Karim Hériché, Franck Lebrin, Thierry Rabilloud, Didier Leroy, * Edmond M. Chambaz, Yves Goldberg dagger

Timely deactivation of kinase cascades is crucial to the normal control of cell signaling and is partly accomplished by protein phosphatase 2A (PP2A). The catalytic (alpha ) subunit of the serine-threonine kinase casein kinase 2 (CK2) bound to PP2A in vitro and in mitogen-starved cells; binding required the integrity of a sequence motif common to CK2alpha and SV40 small t antigen. Overexpression of CK2alpha resulted in deactivation of mitogen-activated protein kinase kinase (MEK) and suppression of cell growth. Moreover, CK2alpha inhibited the transforming activity of oncogenic Ras, but not that of constitutively activated MEK. Thus, CK2alpha may regulate the deactivation of the mitogen-activated protein kinase pathway.

J.-K. Hériché, F. Lebrin, D. Leroy, E. M. Chambaz, Y. Goldberg, Commissariat à l'Energie Atomique, Département de Biologie Moléculaire et Structurale, Laboratoire de Biochimie des Régulations Cellulaires Endocrines, and Institut National de la Santé et de la Recherche Médicale, Unité 244, 17 avenue des Martyrs, F-38054 Grenoble Cédex 9, France.
T. Rabilloud, Commissariat à l'Energie Atomique, Département de Biologie Moléculaire et Structurale, Laboratoire de Bioénergétique Cellulaire et Pathologique, 17 avenue des Martyrs, F-38054 Grenoble Cédex 9, France.
*   Present address: Institut Suisse de Recherche sur le Cancer, 155 chemin des Boveresses, CH-1066 Epalinges, Switzerland.

dagger    To whom correspondence should be addressed.

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M. Kanai, C. Mullen, and D. K. Podolsky (1998)
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