کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1934826 | 1050651 | 2008 | 6 صفحه PDF | دانلود رایگان |
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.
Journal: Biochemical and Biophysical Research Communications - Volume 376, Issue 2, 14 November 2008, Pages 439–444