Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 508, Issue 2, Pages 550-555Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2018.11.134
Keywords
Ca2+/calmodulin-dependent protein kinase (CaMK); Phosphorylation; Polysulfidation; Reactive sulfur species (RSS); Redox regulation
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Funding
- JSPS KAKENHI [18101083, 18104853, 15108994]
- Program for the Strategic Research Foundation at Private Universities of the MEXT, Japan [51311012]
- Showa Pharmaceutical University for Young Scientists
- Nagai Memorial Research Scholarship from the Pharmaceutical Society of Japan
- [26111008]
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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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