Zinc binds to and directly inhibits protein phosphatase 2A in vitro

被引:0
|
作者
Yan Xiong [1 ,2 ,3 ,4 ]
Dan-Ju Luo [4 ]
Xiu-Lian Wang [4 ]
Mei Qiu [4 ]
Yang Yang [4 ]
Xiong Yan [4 ]
Jian-Zhi Wang [4 ]
Qi-Fa Ye [1 ,2 ,3 ,5 ]
Rong Liu [4 ,6 ]
机构
[1] Wuhan University
[2] Zhongnan Hospital of Wuhan University
[3] Institute of Hepatobiliary Diseases of Wuhan University,Transplant Center of Wuhan University, Hubei Key Laboratory of Medical Technology on Transplantation
[4] Key Laboratory of Neurological Disease, Ministry of Education, and Department of Pathophysiology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology
[5] The Third Xiangya Hospital of Central South University, Research Center of National Health Ministry on Transplantation Medicine Engineering and Technology
[6] The Institute of Brain Research, Huazhong University of Science and Technology
基金
中国国家自然科学基金;
关键词
zinc; protein phosphatase 2A; direct inhibition;
D O I
暂无
中图分类号
R346 [];
学科分类号
摘要
Zinc induces protein phosphatase 2A(PP2A) inactivation and tau hyperphosphorylation through PP2A(tyrosine 307) phosphorylation in cells and the brain, but whether Zn2+ has a direct inhibitory effect on PP2 A is not clear. Here we explored the effect of Zn2+ on PP2 A and their direct interaction in vitro. The results showed that Zn2+ mimicked the inhibitory effect of okadaic acid on protein phosphatase and prevented tau dephosphorylation in N2 a cell lysates. PP2 A activity assays indicated that a low concentration(10 μmol/L) of Zn2+ inhibited PP2 A directly. Further Zn2+-IDA-agarose affinity binding assays showed that Zn2+ bound to and inhibited PP2Ac(51-270) but not PP2Ac(1-50) or PP2Ac(271-309). Taken together, Zn2+ inhibits PP2 A directly through binding to PP2Ac(51-270) in vitro.
引用
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页码:331 / 337
页数:7
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