Reactive sulfur species impair Ca2+/calmodulin-dependent protein kinase II via polysulfidation

被引：10

作者：

Araki, Shoma ^{[1
]}

Takata, Tsuyoshi ^{[1
]}

Tsuchiya, Yukihiro ^{[1
]}

Watanabe, Yasuo ^{[1
]}

机构：

[1] Showa Pharmaceut Univ, Dept Pharmacol, Machida, Tokyo 1948543, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2019年 / 508卷 / 02期

关键词：

Ca2+/calmodulin-dependent protein kinase (CaMK); Phosphorylation; Polysulfidation; Reactive sulfur species (RSS); Redox regulation; NITRIC-OXIDE SYNTHASE; S-SULFHYDRATION; ACTIVATION; EXPRESSION; STRESS;

D O I：

10.1016/j.bbrc.2018.11.134

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We previously reported that Ca2+/calmodulin-dependent protein kinase II (CaMKII) is inhibited by S-nitrosylation of Cys(6) in cells. Herein, we show that polysulfidation of CaMKII at Cys(6) limits its enzyme activity following reactive sulfur species (RSS) stimulus. In vitro incubation of CaMKII with the RSS donor, Na2S4, induced the inhibition of the enzyme via its polysulfidation. Treatment with dithiothreitol reversed the polysulfidation and the subsequent inhibition. The inhibition of CaMKII by Na2S4 is competitive with ATP but not with the peptide substrate Syntide-2. In transfected cells expressing CaMKII, the enzyme activity decreased upon treatment with Na2S4, whereas cells expressing mutant CaMKII (C6A) were resistant to this treatment. In addition, the endogenous CaMKII was inhibited by treatment with Na2S4 in RAW264.7 murine macrophage cells. These results suggest a novel regulation of CaMKII by RSS via its Cys(6) polysulfidation in cells. (C) 2018 Elsevier Inc. All rights reserved.

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页码：550 / 555

页数：6

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