Phosphorylation by glycogen synthase kinase of inhibitor‐2 does not change its structure in free state

FEBS Letters

Chen, Yi-Chen¹  Chyan, Chia-lin⁵  Tsay, Li-huang³  Jeng, Hao-Hsuan³  Lin, Ta-Hsien⁴  Lin, Fang-Min²  Huang, Hsien-bin³  Tang, Tzu Chun² 

[1] Department of Medical Technology, Tzu Chi University, Hualien 970, Taiwan, ROC;Department of Medical Research and Education, Taipei Veterans General Hospital, Shih-pai, Taipei 112, Taiwan, ROC;Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 621, Taiwan, ROC;Institute of Biochemistry, National Yang-Ming University, Shih-pai, Taipei 112, Taiwan, ROC;Department of Chemistry, National Dong Hwa University, Hualien 974, Taiwan, ROC

关键词: Nuclear magnetic resonance;    Circular dichroism;    Inhibitor-2;    Protein phosphatase-1;    Glycogen synthase kinase-3;   

DOI  :  10.1016/S0014-5793(03)01097-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Inhibitor-2 (I2) is a thermostable protein that specifically binds to the catalytic subunit of protein phosphatase-1 (PP1), resulting in the formation of the inactive holoenzyme, ATP-Mg-dependent phosphatase. Phosphorylation of I2 at Thr-72 by glycogen synthase kinase-3 (GSK-3) results in activation of the phosphatase, suggesting that kinase action triggers conformational change in the complex. In this paper, we characterize the effect of GSK-3 phosphorylation on the structure of free state I2[1–172] by nuclear magnetic resonance and circular dichroism spectroscopy, and show that phosphorylation has no significant effect on its conformation. We conclude that the conformational changes of ATP-Mg-dependent phosphatase induced by GSK-3 phosphorylation must depend on the interactions between PP1 and I2.

【 授权许可】

Unknown