Naotada Ishihara

Summary

Affiliation: Kyushu University
Country: Japan

Publications

  1. ncbi request reprint [Mitochondrial dynamics regulated by fusion and fission]
    Naotada Ishihara
    Tanpakushitsu Kakusan Koso 50:931-9. 2005
  2. ncbi request reprint [Mitochondrial fusion and fission in mammalian cells]
    Naotada Ishihara
    Tanpakushitsu Kakusan Koso 50:1868-71. 2005
  3. ncbi request reprint Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission
    Naoko Taguchi
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812 8582, Japan
    J Biol Chem 282:11521-9. 2007
  4. ncbi request reprint Identification of a novel protein that regulates mitochondrial fusion by modulating mitofusin (Mfn) protein function
    Yuka Eura
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812 8582, Japan
    J Cell Sci 119:4913-25. 2006
  5. doi request reprint Characterization of the mitochondrial protein LETM1, which maintains the mitochondrial tubular shapes and interacts with the AAA-ATPase BCS1L
    Shoko Tamai
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Japan
    J Cell Sci 121:2588-600. 2008
  6. pmc Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space
    Hidenori Otera
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Japan
    EMBO J 24:1375-86. 2005
  7. ncbi request reprint Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
    Naotada Ishihara
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812 8582, Japan
    J Cell Sci 117:6535-46. 2004
  8. ncbi request reprint Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion
    Yuka Eura
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812 8582
    J Biochem 134:333-44. 2003
  9. ncbi request reprint Regulation of mitochondrial morphology by membrane potential, and DRP1-dependent division and FZO1-dependent fusion reaction in mammalian cells
    Naotada Ishihara
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, 812 8582, Fukuoka, Japan
    Biochem Biophys Res Commun 301:891-8. 2003
  10. ncbi request reprint Analysis of functional domains of rat mitochondrial Fis1, the mitochondrial fission-stimulating protein
    Akihiro Jofuku
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812 8582, Japan
    Biochem Biophys Res Commun 333:650-9. 2005

Collaborators

  • Katsuyoshi Mihara
  • N Mizushima
  • Y Ohsumi
  • Yuka Eura
  • Toshihiko Oka
  • Akihiro Jofuku
  • Shoko Tamai
  • Naoko Taguchi
  • Sadaki Yokota
  • Hidenori Otera
  • Akiko Kuma
  • Tomoko Sayano
  • Hiroshi Iida
  • Shoko Kiguchiya
  • Jun Ichi Hayashi
  • Zen ichiro Nagaura
  • Shigenori Ohsakaya

Detail Information

Publications12

  1. ncbi request reprint [Mitochondrial dynamics regulated by fusion and fission]
    Naotada Ishihara
    Tanpakushitsu Kakusan Koso 50:931-9. 2005
  2. ncbi request reprint [Mitochondrial fusion and fission in mammalian cells]
    Naotada Ishihara
    Tanpakushitsu Kakusan Koso 50:1868-71. 2005
  3. ncbi request reprint Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission
    Naoko Taguchi
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812 8582, Japan
    J Biol Chem 282:11521-9. 2007
    ..Exogenous expression of unphosphorylated mutant Drp1S585A led to reduced mitotic mitochondrial fragmentation. These results suggest that phosphorylation of Drp1 on Ser-585 promotes mitochondrial fission in mitotic cells...
  4. ncbi request reprint Identification of a novel protein that regulates mitochondrial fusion by modulating mitofusin (Mfn) protein function
    Yuka Eura
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812 8582, Japan
    J Cell Sci 119:4913-25. 2006
    ..Together, these findings suggest that MIB is essential for cellular function by regulating mitochondrial membrane dynamics in cooperation with Mfn proteins...
  5. doi request reprint Characterization of the mitochondrial protein LETM1, which maintains the mitochondrial tubular shapes and interacts with the AAA-ATPase BCS1L
    Shoko Tamai
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Japan
    J Cell Sci 121:2588-600. 2008
    ..BCS1L knockdown caused disassembly of the respiratory chains as well as LETM1 downregulation and induced distinct changes in mitochondrial morphology...
  6. pmc Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space
    Hidenori Otera
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Japan
    EMBO J 24:1375-86. 2005
    ..The results also suggest the presence of a unique protease that is regulated by proapoptotic stimuli in caspase-independent cell death...
  7. ncbi request reprint Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity
    Naotada Ishihara
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812 8582, Japan
    J Cell Sci 117:6535-46. 2004
    ..These findings indicate that the two Mfn proteins have distinct activities, and suggest that Mfn1 is mainly responsible for GTP-dependent membrane tethering...
  8. ncbi request reprint Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion
    Yuka Eura
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812 8582
    J Biochem 134:333-44. 2003
    ..We conclude that the two Mfn isoforms cooperate in mitochondrial fusion in mammalian cells...
  9. ncbi request reprint Regulation of mitochondrial morphology by membrane potential, and DRP1-dependent division and FZO1-dependent fusion reaction in mammalian cells
    Naotada Ishihara
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, 812 8582, Fukuoka, Japan
    Biochem Biophys Res Commun 301:891-8. 2003
    ..Furthermore, a HVJ-dependent cell fusion assay combined with RNA interference (RNAi) demonstrated that both FZO1 isoforms are essential and must be acting in cis for the mitochondrial fusion reaction to occur...
  10. ncbi request reprint Analysis of functional domains of rat mitochondrial Fis1, the mitochondrial fission-stimulating protein
    Akihiro Jofuku
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka 812 8582, Japan
    Biochem Biophys Res Commun 333:650-9. 2005
    ..Any mutations that disturb the proper oligomeric assembly compromise mitochondrial division-stimulating activity of rFis1...
  11. pmc Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
    Naotada Ishihara
    Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, Fukuoka, Japan
    EMBO J 25:2966-77. 2006
    ..Thus, mammalian mitochondrial function and morphology is regulated through processing of OPA1 in a DeltaPsi-dependent manner...
  12. ncbi request reprint Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast
    Akiko Kuma
    Department of Cell Biology, National Institute for Basic Biology, 38 Nishigonaka, Myodaiji, Okazaki 444 8585, Japan
    J Biol Chem 277:18619-25. 2002
    ..These results suggest that the Apg12-Apg5 conjugate and Apg16 form a multimeric complex mediated by the Apg16 homo-oligomer, and formation of the approximately 350-kDa complex is required for autophagy in yeast...