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

Ta Hsien Lin, Yi Chen Chen, Chia Lin Chyan, Li Huang Tsay, Tzu Chun Tang, Hao Hsuan Jeng, Fang Min Lin, Hsien Bin Huang*

*此作品的通信作者

研究成果: Article同行評審

8 引文 斯高帕斯(Scopus)

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.

原文English
頁(從 - 到)253-256
頁數4
期刊FEBS Letters
554
發行號3
DOIs
出版狀態Published - 20 11月 2003

指紋

深入研究「Phosphorylation by glycogen synthase kinase of inhibitor-2 does not change its structure in free state」主題。共同形成了獨特的指紋。

引用此