Götz C, Wagner P, Issinger O G, Montenarh M
Institute of Medical Biochemistry, University of the Saarland, Homburg, Germany.
Oncogene. 1996 Jul 18;13(2):391-8.
p21WAF1/CIP1 which belongs to a class of regulatory proteins that interact with cyclin dependent kinases is a potent inhibitor of these kinases. The inhibition of the cyclin dependent kinases induces an arrest of cells in the G phase of the cell cycle. In addition p21WAF1/CIP1 associates with PCNA and inhibits DNA replication. Here, we show that p21WAF1/CIP1 binds to the regulatory beta-subunit of protein kinase CK2 but not to the catalytic alpha-subunit. Binding of p21WAF1/CIP1 down regulates the kinase activity of CK2 with respect to the phosphorylation of the beta-subunit of CK2, casein and the C-terminus of p53. This study demonstrates a new binding partner for the regulatory beta-subunit of protein kinase CK2 which regulates the activity of the holoenzyme.
属于与细胞周期蛋白依赖性激酶相互作用的一类调节蛋白的p21WAF1/CIP1是这些激酶的有效抑制剂。细胞周期蛋白依赖性激酶的抑制会导致细胞在细胞周期的G期停滞。此外，p21WAF1/CIP1与增殖细胞核抗原（PCNA）结合并抑制DNA复制。在此，我们表明p21WAF1/CIP1与蛋白激酶CK2的调节β亚基结合，但不与催化α亚基结合。p21WAF1/CIP1的结合下调了CK2对CK2β亚基、酪蛋白和p53 C末端磷酸化的激酶活性。这项研究证明了蛋白激酶CK2调节β亚基的一种新结合伴侣，该伴侣调节全酶的活性。
