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Characterization of the InsP6-dependent interaction between CK2 and Nopp140 |
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| Authors: | Lee Won-Kyu Lee Sang-Yeop Kim Woo-Il Rho Yoon-Hwa Bae Young-Seuk Lee Cheolju Kim Ick Young Yu Yeon Gyu |
| Affiliation: | a Department of Chemistry, Kookmin University, 861-1, Jeoungneung-dong, Songbuk-gu, 136-702, Seoul, Republic of Korea b Division of Life Sciences, Korea Institute of Science and Technology, 39-1, Hawolgok-dong, Songbuk-gu, 136-791, Seoul, Republic of Korea c Department of Biochemistry, Kyungpook National University, Daegu 702-701, Republic of Korea d Laboratory of Cellular and Molecular Biochemistry, School of Life Science and Biotechnology, Korea University, 5th street, Anam-dong, Songbuk-gu, 136-701, Seoul, Republic of Korea |
| Abstract: | Nopp140, a highly phosphorylated nucleolar protein, negatively regulates CK2, a kinase essential for cell proliferation. We quantitatively analyzed the interaction between two subunits of CK2 and Nopp140 and characterized the mechanism by which InsP6 inhibits the interaction. Nopp140 specifically binds to the catalytic subunit of CK2 (CK2α) with a dissociation constant of (Kd) of 4 nM, which interferes with the catalytic activity of CK2. The C-terminal region of Nopp140 is determined as CK2α-binding region by a yeast two-hybrid method as well as a direct measurement of the interaction between CK2α and deletion mutants of Nopp140. InsP6 specifically binds to CK2α and disrupts the interaction between CK2α and Nopp140 with an IC50 value of 25 μM, thereby attenuating the Nopp140-mediated repression of CK2 activity. |
| Keywords: | CK2 Nopp140 InsP6 Protein interaction |
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