Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Hidenori Otera"'
MAVS is energized by Mff which senses mitochondrial metabolism via AMPK for acute antiviral immunity
Autor:
Yuki Hanada, Naotada Ishihara, Lixiang Wang, Hidenori Otera, Takaya Ishihara, Takumi Koshiba, Katsuyoshi Mihara, Yoshihiro Ogawa, Masatoshi Nomura
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Mitochondrial antiviral signalling protein (MAVS) is an adaptor of RIG-I like receptor. Here the authors show that mitochondrial fission factor (Mff) is required for clustering of MAVS on the outer mitochondrial membrane during antiviral response.
Externí odkaz:
https://doaj.org/article/46f3aca185b54918aa1eae68e9fb7b4e
Autor:
Hidenori Otera, Katsuyoshi Mihara
Publikováno v:
International Journal of Cell Biology, Vol 2012 (2012)
Mitochondria participate in a variety of physiologic processes, such as ATP production, lipid metabolism, iron-sulfur cluster biogenesis, and calcium buffering. The morphology of mitochondria changes dynamically due to their frequent fusion and divis
Externí odkaz:
https://doaj.org/article/275f765031a9454ba7ceddf68b0f929a
Autor:
Kentaro Furukawa, Tetsu Saigusa, Yasuyoshi Sakai, Shun-ichi Yamashita, Xiulian Jin, Hidenori Otera, Akiko Nezu, Tomotake Kanki, Maho Hamasaki, Tamotsu Yoshimori, Katsuyoshi Mihara
Publikováno v:
The Journal of Cell Biology
It remains controversial whether Dnm1/Drp1-mediated mitochondrial division is essential for mitophagy. Yamashita et al. show that Dnm1/Drp1-independent mitochondrial division occurs after formation of isolation membranes and in cooperation with autop
Publikováno v:
Antioxidants & Redox Signaling. 19:389-399
Mitochondria are double membrane-bound organelles with tubular network structures that are essential for oxidative ATP production and play pivotal roles in regulating calcium homeostasis and apoptosis. Furthermore, mitochondria produce large amounts
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1833:1256-1268
Mitochondrial morphology changes dynamically by coordinated fusion and fission and cytoskeleton-based transport. Cycles of outer and inner membrane fusion and fission are required for the exchange of damaged mitochondrial genome DNA, proteins, and li
Autor:
Yukio Fujiki, Hidenori Otera
Publikováno v:
Traffic. 13:1364-1377
Human catalase forms a 240-kDa tetrameric complex and degrades H2O2 in peroxisomes. Human catalase is targeted to peroxisomes by the interaction of its peroxisomal targeting signal type 1 (PTS1)-like KANL sequence with the cytosolic PTS1 receptor Pex
Autor:
Katsuyoshi Mihara, Hidenori Otera
Publikováno v:
Small GTPases. 2:167-172
Mitochondria frequently change their morphology by fusion and fission, and these dynamic morphologic changes are essential for maintaining both mitochondrial and cellular functions. The cytoplasmic dynamin-related guanosine triphosphatase (GTPase) Dr
Autor:
Hidenori Otera, Katsuyoshi Mihara
Publikováno v:
Journal of Biochemistry. 149:241-251
Mitochondria are highly dynamic organelles that continuously change their shape through frequent fusion, fission and movement throughout the cell, and these dynamics are crucial for the life and death of the cells as they have been linked to apoptosi
Autor:
Megan M. Cleland, Chunxin Wang, Richard J. Youle, Sadaki Yokota, Kiyoko Setoguchi, Hidenori Otera, Katsuyoshi Mihara
Publikováno v:
The Journal of Cell Biology
Localization of the dynamin-related GTPase Drp1 to mitochondria relies on the mitochondrial fission factor Mff.
The cytoplasmic dynamin-related guanosine triphosphatase Drp1 is recruited to mitochondria and mediates mitochondrial fission. Althou
The cytoplasmic dynamin-related guanosine triphosphatase Drp1 is recruited to mitochondria and mediates mitochondrial fission. Althou
Autor:
Maki Maeda, Katsuyoshi Mihara, Yu-ichi Goto, Akihiro Jofuku, Naoko Taguchi, Satoshi O. Suzuki, Hidetaka Morinaga, Naotada Ishihara, Keiji Masuda, Sadaki Yokota, Ryoichi Takayanagi, Hiroki Kato, Hidenori Otera, Masatoshi Nomura, Yae Nakanishi, Ikuya Nonaka
Publikováno v:
Nature Cell Biology. 11:958-966
Mitochondrial morphology is dynamically controlled by a balance between fusion and fission. The physiological importance of mitochondrial fission in vertebrates is less clearly defined than that of mitochondrial fusion. Here we show that mice lacking