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

Bo, Tomoki; Yamamori, Tohru; Suzuki, Motofumi; Sakai, Yuri; Yamamoto, Kumiko; Inanami, Osamu

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

Bo, Tomoki; Yamamori, Tohru; Suzuki, Motofumi et al.

Biochemical and biophysical research communications, 2018, 295(2), 1601-1607

Permalink : https://hdl.handle.net/2115/72273

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アクセス権	open access
URI	https://hdl.handle.net/2115/72273
タイトル	Calmodulin-dependent protein kinase II (CaMKII) mediates radiation-induced mitochondrial fission by regulating the phosphorylation of dynamin-related protein 1 (Drp1) at serine 616
著者	Bo, Tomoki ; Yamamori, Tohru ; Suzuki, Motofumi ; Sakai, Yuri ; Yamamoto, Kumiko ; Inanami, Osamu
著者名 Bo, Tomoki
e-Rad_Researcher 00512675 著者名 Yamamori, Tohru
著者名 Suzuki, Motofumi
著者名 Sakai, Yuri
著者名 Yamamoto, Kumiko
e-Rad_Researcher 10193559 著者名 Inanami, Osamu
言語	英語
キーワード	CaMKII
	Drp1
	Ionizing radiation
	Mitochondrial dynamics
	Phosphorylation
発行日	2018-01-08
出版者	Elsevier
収録物名	Biochemical and biophysical research communications
巻(号)	295(2)
ページ	1601-1607
抄録	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.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
権利情報	© 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/
PISSN	0006-291X
関連情報	PMID 29217195
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1016/j.bbrc.2017.12.012