Regulation of Protein Phosphatase 2A by Direct Interaction with Casein Kinase 2α-Reference-Cited by-同舟云学术

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

Published:1997-05-09 Issue:5314 Volume:276 Page:952-955
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Hériché Jean-Karim¹²,Lebrin Franck¹²,Rabilloud Thierry¹²,Leroy Didier¹²,Chambaz Edmond M.¹²,Goldberg Yves¹²

Affiliation:

1. 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.

2. 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.

Abstract

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 (α) 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 CK2α and SV40 small t antigen. Overexpression of CK2α resulted in deactivation of mitogen-activated protein kinase kinase (MEK) and suppression of cell growth. Moreover, CK2α inhibited the transforming activity of oncogenic Ras, but not that of constitutively activated MEK. Thus, CK2α may regulate the deactivation of the mitogen-activated protein kinase pathway.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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