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Calmodulin-dependent protein kinase II (CaMKII) mediates radiation-induced mitochondrial fission by regulating the phosphorylation of dynamin-related protein 1 (Drp1) at serine 616

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Title: Calmodulin-dependent protein kinase II (CaMKII) mediates radiation-induced mitochondrial fission by regulating the phosphorylation of dynamin-related protein 1 (Drp1) at serine 616
Authors: Bo, Tomoki Browse this author
Yamamori, Tohru Browse this author →KAKEN DB
Suzuki, Motofumi Browse this author
Sakai, Yuri Browse this author
Yamamoto, Kumiko Browse this author
Inanami, Osamu Browse this author →KAKEN DB
Keywords: CaMKII
Drp1
Ionizing radiation
Mitochondrial dynamics
Phosphorylation
Issue Date: 8-Jan-2018
Publisher: Elsevier
Journal Title: Biochemical and biophysical research communications
Volume: 295
Issue: 2
Start Page: 1601
End Page: 1607
Publisher DOI: 10.1016/j.bbrc.2017.12.012
PMID: 29217195
Abstract: Mitochondrial dynamics are suggested to be indispensable for the maintenance of cellular quality and function in response to various stresses. While ionizing radiation (IR) stimulates mitochondrial fission, which is mediated by the mitochondrial fission protein, dynamin-related protein 1 (Drp1), it remains unclear how IR promotes Drp1 activation and subsequent mitochondrial fission. Therefore, we conducted this study to investigate these concerns. First, we found that X-irradiation triggered Drp1 phosphorylation at serine 616 (S616) but not at serine 637 (S637). Reconstitution analysis revealed that introduction of wild-type (WT) Drp1 recovered radiation-induced mitochondrial fission, which was absent in Drp1-deficient cells. Compared with cells transfected with WT or S637A Drp1, the change in mitochondrial shape following irradiation was mitigated in S616A Drp1-transfected cells. Furthermore, inhibition of CaMKII significantly suppressed Drp1 5616 phosphorylation and mitochondrial fission induced by IR. These results suggest that Drp1 phosphorylation at S616, but not at 5637, is prerequisite for radiation induced mitochondrial fission and that CaMKII regulates Drp1 phosphorylation at 5616 following irradiation. (C) 2017 Elsevier Inc. All rights reserved.
Rights: © 2018. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
http://creativecommons.org/licenses/by-nc-nd/4.0/
Type: article (author version)
URI: http://hdl.handle.net/2115/72273
Appears in Collections:獣医学院・獣医学研究院 (Graduate School of Veterinary Medicine / Faculty of Veterinary Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 稲波 修

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