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Mammalian Homologue NME3 of DYNAMO1 Regulates Peroxisome Division

Medical Institute of Bioregulation, Institute of Rheological Functions of Food—Kyushu University Collaboration Program, Kyushu University, 3-1-1 Maidashi, Fukuoka 812-8582, Japan
Faculty of Arts and Science, Kyushu University, 744 Motooka, Fukuoka 819-0395, Japan
Department of Cell Biology, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, USA
Institute of Molecular Medicine, College of Medicine, National Taiwan University, Taipei 10002, Taiwan
Galilee Medical Center, Institute of Human Genetics, Nahariya 22100, Israel
Azrieli Faculty of Medicine, Bar-Ilan University, Safed 13100, Israel
Author to whom correspondence should be addressed.
These authors equally contributed to this work.
Present address: Department of Neuroinflammation and Brain Fatigue Science, Graduate School of Medical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan.
Present address: Institute of Rheological Function of Food, Hisayama-cho, Fukuoka 811-2501, Japan.
Int. J. Mol. Sci. 2020, 21(21), 8040;
Received: 8 September 2020 / Revised: 22 October 2020 / Accepted: 25 October 2020 / Published: 28 October 2020
Peroxisomes proliferate by sequential processes comprising elongation, constriction, and scission of peroxisomal membrane. It is known that the constriction step is mediated by a GTPase named dynamin-like protein 1 (DLP1) upon efficient loading of GTP. However, mechanism of fuelling GTP to DLP1 remains unknown in mammals. We earlier show that nucleoside diphosphate (NDP) kinase-like protein, termed dynamin-based ring motive-force organizer 1 (DYNAMO1), generates GTP for DLP1 in a red alga, Cyanidioschyzon merolae. In the present study, we identified that nucleoside diphosphate kinase 3 (NME3), a mammalian homologue of DYNAMO1, localizes to peroxisomes. Elongated peroxisomes were observed in cells with suppressed expression of NME3 and fibroblasts from a patient lacking NME3 due to the homozygous mutation at the initiation codon of NME3. Peroxisomes proliferated by elevation of NME3 upon silencing the expression of ATPase family AAA domain containing 1, ATAD1. In the wild-type cells expressing catalytically-inactive NME3, peroxisomes were elongated. These results suggest that NME3 plays an important role in peroxisome division in a manner dependent on its NDP kinase activity. Moreover, the impairment of peroxisome division reduces the level of ether-linked glycerophospholipids, ethanolamine plasmalogens, implying the physiological importance of regulation of peroxisome morphology. View Full-Text
Keywords: peroxisome; constriction; NDP kinase; GTP; nme3 patient peroxisome; constriction; NDP kinase; GTP; nme3 patient
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MDPI and ACS Style

Honsho, M.; Abe, Y.; Imoto, Y.; Chang, Z.-F.; Mandel, H.; Falik-Zaccai, T.C.; Fujiki, Y. Mammalian Homologue NME3 of DYNAMO1 Regulates Peroxisome Division. Int. J. Mol. Sci. 2020, 21, 8040.

AMA Style

Honsho M, Abe Y, Imoto Y, Chang Z-F, Mandel H, Falik-Zaccai TC, Fujiki Y. Mammalian Homologue NME3 of DYNAMO1 Regulates Peroxisome Division. International Journal of Molecular Sciences. 2020; 21(21):8040.

Chicago/Turabian Style

Honsho, Masanori, Yuichi Abe, Yuuta Imoto, Zee-Fen Chang, Hanna Mandel, Tzipora C. Falik-Zaccai, and Yukio Fujiki. 2020. "Mammalian Homologue NME3 of DYNAMO1 Regulates Peroxisome Division" International Journal of Molecular Sciences 21, no. 21: 8040.

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