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

作者：Jean-Karim Hèriché, Franck Lebrin, Thierry Rabilloud, Didier Leroy, EDMOND M. CHAMBAZ, Yves Goldberg · 发表于：Science · 年份：1997 · DOI：10.1126/science.276.5314.952 · 被引用次数：271 · 研究领域：Enzyme Production and Characterization、Protein Kinase Regulation and GTPase Signaling、Phytase and its Applications

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.