K
Katsuyoshi Mihara
Researcher at Kyushu University
Publications - 103
Citations - 12982
Katsuyoshi Mihara is an academic researcher from Kyushu University. The author has contributed to research in topics: Mitochondrion & Mitochondrial fission. The author has an hindex of 55, co-authored 103 publications receiving 11473 citations. Previous affiliations of Katsuyoshi Mihara include Boston Children's Hospital & Kurume University.
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Journal ArticleDOI
Mitotic Phosphorylation of Dynamin-related GTPase Drp1 Participates in Mitochondrial Fission
TL;DR: Results suggest that phosphorylation of Drp1 on Ser-585 promotes mitochondrial fission in mitotic cells, and exogenous expression of unphosphorylated mutantDrp1S585A led to reduced mitotic mitochondrial fragmentation.
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Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells.
Hidenori Otera,Chunxin Wang,Megan M. Cleland,Kiyoko Setoguchi,Sadaki Yokota,Richard J. Youle,Katsuyoshi Mihara +6 more
TL;DR: Localization of the dynamin-related GTPase Drp1 to mitochondria relies on the mitochondrial fission factor Mff.
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Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice
Naotada Ishihara,Masatoshi Nomura,Akihiro Jofuku,Hiroki Kato,Satoshi O. Suzuki,Keiji Masuda,Hidenori Otera,Yae Nakanishi,Ikuya Nonaka,Yu-ichi Goto,Naoko Taguchi,Hidetaka Morinaga,Maki Maeda,Ryoichi Takayanagi,Sadaki Yokota,Katsuyoshi Mihara +15 more
TL;DR: Drp1−/− murine embryonic fibroblasts and embryonic stem cells revealed that Drp1 is required for a normal rate of cytochrome c release and caspase activation during apoptosis, although mitochondrial outer membrane permeabilization, as examined by the release of Smac/Diablo and Tim8a, may occur independently of Drp 1 activity.
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Regulation of mitochondrial morphology through proteolytic cleavage of OPA1.
TL;DR: M mammalian mitochondrial function and morphology is regulated through processing of OPA1 in a ΔΨ‐dependent manner through proteolytic cleavage of Mgm1, the yeast homolog of O PA1.
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Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity.
TL;DR: Findings indicate that the two Mfn proteins have distinct activities, and suggest that Mfn1 is mainly responsible for GTP-dependent membrane tethering.