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Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission
Author(s): Taguchi N (Taguchi, Naoko), Ishihara N (Ishihara, Naotada), Jofuku A (Jofuku, Akihiro), Oka T (Oka, Toshihiko), Mihara K (Mihara, Katsuyoshi)
Source: JOURNAL OF BIOLOGICAL CHEMISTRY    Volume: 282    Issue: 15    Pages: 11521-11529    Published: APR 13 2007  
Times Cited: 63     References: 49     
Abstract: Organelles are inherited to daughter cells beyond dynamic changes of the membrane structure during mitosis. Mitochondria are dynamic entities, frequently dividing and fusing with each other, during which dynamin-related GTPase Drp1 is required for the fission reaction. In this study, we analyzed mitochondrial dynamics in mitotic mammalian cells. Although mitochondria in interphase HeLa cells are long tubular network structures, they are fragmented in early mitotic phase, and the filamentous network structures are subsequently reformed in the daughter cells. In marked contrast, tubular mitochondrial structures are maintained during mitosis in Drp1 knockdown cells, indicating that the mitochondrial fragmentation in mitosis requires mitochondrial fission by Drp1. Drp1 was specifically phosphorylated in mitosis by Cdk1/cyclin B on Ser-585. Exogenous expression of unphosphorylated mutant Drp1(S585A) led to reduced mitotic mitochondrial fragmentation. These results suggest that phosphorylation of Drp1 on Ser-d585 promotes mitochondrial fission in mitotic cells.
Document Type: Article
Language: English
Reprint Address: Mihara, K (reprint author), Kyushu Univ, Grad Sch Med Sci, Dept Mol Biol, Higashi Ku, 3-1-1 Maidashi, Fukuoka 8128582, Japan
Addresses:
1. Kyushu Univ, Grad Sch Med Sci, Dept Mol Biol, Higashi Ku, Fukuoka 8128582, Japan
Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA
Subject Category: Biochemistry & Molecular Biology
IDS Number: 160LG
ISSN: 0021-9258
DOI: 10.1074/jbc.M607279200
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