TY - JOUR
T1 - COX assembly factor ccdc56 regulates mitochondrial morphology by affecting mitochondrial recruitment of Drp1
AU - Ban-Ishihara, Reiko
AU - Tomohiro-Takamiya, Shiho
AU - Tani, Motohiro
AU - Baudier, Jacques
AU - Ishihara, Naotada
AU - Kuge, Osamu
N1 - Funding Information:
We wish to thank Katsuyoshi Mihara and Toshihiko Oka for the antibodies, and Tadashi Ogishima, Sakae Kitada and Daniel Ken Inaoka for the discussions. This work was supported by Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology of Japan (Grant Nos. 195900681 to O.K., 26291044 and 26111522 to N.I., 15K18534 to R.B.-I.).
Publisher Copyright:
© 2015 Federation of European Biochemical Societies.
PY - 2015/10/7
Y1 - 2015/10/7
N2 - Mitochondria are dynamic organelles that alter their morphology in response to cellular signaling and differentiation through balanced fusion and fission. In this study, we found that the mitochondrial inner membrane ATPase ATAD3A interacted with ccdc56/MITRAC12/COA3, a subunit of the cytochrome oxidase (COX)-assembly complex. Overproduction of ccdc56 in HeLa cells resulted in fragmented mitochondrial morphology, while mitochondria were highly elongated in ccdc56-repressed cells by the defective recruitment of the fission factor Drp1. We also found that mild and chronic inhibition of COX led to mitochondrial elongation, as seen in ccdc56-repressed cells. These results indicate that ccdc56 positively regulates mitochondrial fission via regulation of COX activity and the mitochondrial recruitment of Drp1, and thus, suggest a novel relationship between COX assembly and mitochondrial morphology.
AB - Mitochondria are dynamic organelles that alter their morphology in response to cellular signaling and differentiation through balanced fusion and fission. In this study, we found that the mitochondrial inner membrane ATPase ATAD3A interacted with ccdc56/MITRAC12/COA3, a subunit of the cytochrome oxidase (COX)-assembly complex. Overproduction of ccdc56 in HeLa cells resulted in fragmented mitochondrial morphology, while mitochondria were highly elongated in ccdc56-repressed cells by the defective recruitment of the fission factor Drp1. We also found that mild and chronic inhibition of COX led to mitochondrial elongation, as seen in ccdc56-repressed cells. These results indicate that ccdc56 positively regulates mitochondrial fission via regulation of COX activity and the mitochondrial recruitment of Drp1, and thus, suggest a novel relationship between COX assembly and mitochondrial morphology.
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U2 - 10.1016/j.febslet.2015.08.039
DO - 10.1016/j.febslet.2015.08.039
M3 - Article
C2 - 26358295
AN - SCOPUS:84943197220
VL - 589
SP - 3126
EP - 3132
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 20
M1 - 37349
ER -