Nobuko Matsushita - Academia.edu (original) (raw)
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Papers by Nobuko Matsushita
10.1128/MCB.23.15.5421-5430.2003. 2003, 23(15):5421. DOI: Mol. Cell. Biol. Minoru Takata Mitsune ... more 10.1128/MCB.23.15.5421-5430.2003. 2003, 23(15):5421. DOI: Mol. Cell. Biol. Minoru Takata Mitsune Tanimoto, Mine Harada, Larry H. Thompson and Hiroshi Arakawa, Jane E. Lamerdin, Jean-Marie Buerstedde, Kazuhiko Yamamoto, Masamichi Ishiai, Nobuko Matsushita, Recombination in Vertebrate Cells Double-Strand Breaks by Homologous Radiationand Enzyme-Induced DNA Fanconi Anemia FANCG Protein in Mitigating
Life Science Alliance
Mitochondrial abnormalities are associated with developmental disorders, although a causal relati... more Mitochondrial abnormalities are associated with developmental disorders, although a causal relationship remains largely unknown. Here, we report that increased oxidative stress in neurons by deletion of mitochondrial ubiquitin ligase MITOL causes a potential neuroinflammation including aberrant astrogliosis and microglial activation, indicating that mitochondrial abnormalities might confer a risk for inflammatory diseases in brain such as psychiatric disorders. A role of MITOL in both mitochondrial dynamics and ER-mitochondria tethering prompted us to characterize three-dimensional structures of mitochondria in vivo. In MITOL-deficient neurons, we observed a significant reduction in the ER-mitochondria contact sites, which might lead to perturbation of phospholipids transfer, consequently reduce cardiolipin biogenesis. We also found that branched large mitochondria disappeared by deletion of MITOL. These morphological abnormalities of mitochondria resulted in enhanced oxidative stre...
Molecular cell
In DNA damage responses, the Fanconi anemia (FA) protein, FancD2, is targeted to chromatin and fo... more In DNA damage responses, the Fanconi anemia (FA) protein, FancD2, is targeted to chromatin and forms nuclear foci following its monoubiquitination, a process likely catalyzed by the FA core complex. Here, we show that a chicken FancD2-ubiquitin fusion protein, carrying a ...
Molecular and Cellular Biology, 2004
The yeast SNM1/PSO2 gene specifically functions in DNA interstrand cross-link (ICL) repair, and i... more The yeast SNM1/PSO2 gene specifically functions in DNA interstrand cross-link (ICL) repair, and its role has been suggested to be separate from other DNA repair pathways. In vertebrates, there are three homologs of SNM1 (SNM1A, SNM1B, and SNM1C/Artemis; SNM1 family proteins) whose functions are largely unknown. We disrupted each of the SNM1 family genes in the chicken B-cell line DT40. Both SNM1A-and SNM1B-deficient cells were sensitive to cisplatin but not to X-rays, whereas SNM1C/Artemis-deficient cells exhibited sensitivity to X-rays but not to cisplatin. SNM1A was nonepistatic with XRCC3 (homologous recombination), RAD18 (translesion synthesis), FANCC (Fanconi anemia), and SNM1B in ICL repair. SNM1A protein formed punctate nuclear foci depending on the conserved SNM1 (metallo--lactamase) domain. PIAS1 was found to physically interact with SNM1A, and they colocalized at nuclear foci. Point mutations in the SNM1 domain, which disrupted the interaction with PIAS1, led to mislocalization of SNM1A in the nucleus and loss of complementation of snm1a cells. These results suggest that interaction between SNM1A and PIAS1 is required for ICL repair.
10.1128/MCB.23.15.5421-5430.2003. 2003, 23(15):5421. DOI: Mol. Cell. Biol. Minoru Takata Mitsune ... more 10.1128/MCB.23.15.5421-5430.2003. 2003, 23(15):5421. DOI: Mol. Cell. Biol. Minoru Takata Mitsune Tanimoto, Mine Harada, Larry H. Thompson and Hiroshi Arakawa, Jane E. Lamerdin, Jean-Marie Buerstedde, Kazuhiko Yamamoto, Masamichi Ishiai, Nobuko Matsushita, Recombination in Vertebrate Cells Double-Strand Breaks by Homologous Radiationand Enzyme-Induced DNA Fanconi Anemia FANCG Protein in Mitigating
Life Science Alliance
Mitochondrial abnormalities are associated with developmental disorders, although a causal relati... more Mitochondrial abnormalities are associated with developmental disorders, although a causal relationship remains largely unknown. Here, we report that increased oxidative stress in neurons by deletion of mitochondrial ubiquitin ligase MITOL causes a potential neuroinflammation including aberrant astrogliosis and microglial activation, indicating that mitochondrial abnormalities might confer a risk for inflammatory diseases in brain such as psychiatric disorders. A role of MITOL in both mitochondrial dynamics and ER-mitochondria tethering prompted us to characterize three-dimensional structures of mitochondria in vivo. In MITOL-deficient neurons, we observed a significant reduction in the ER-mitochondria contact sites, which might lead to perturbation of phospholipids transfer, consequently reduce cardiolipin biogenesis. We also found that branched large mitochondria disappeared by deletion of MITOL. These morphological abnormalities of mitochondria resulted in enhanced oxidative stre...
Molecular cell
In DNA damage responses, the Fanconi anemia (FA) protein, FancD2, is targeted to chromatin and fo... more In DNA damage responses, the Fanconi anemia (FA) protein, FancD2, is targeted to chromatin and forms nuclear foci following its monoubiquitination, a process likely catalyzed by the FA core complex. Here, we show that a chicken FancD2-ubiquitin fusion protein, carrying a ...
Molecular and Cellular Biology, 2004
The yeast SNM1/PSO2 gene specifically functions in DNA interstrand cross-link (ICL) repair, and i... more The yeast SNM1/PSO2 gene specifically functions in DNA interstrand cross-link (ICL) repair, and its role has been suggested to be separate from other DNA repair pathways. In vertebrates, there are three homologs of SNM1 (SNM1A, SNM1B, and SNM1C/Artemis; SNM1 family proteins) whose functions are largely unknown. We disrupted each of the SNM1 family genes in the chicken B-cell line DT40. Both SNM1A-and SNM1B-deficient cells were sensitive to cisplatin but not to X-rays, whereas SNM1C/Artemis-deficient cells exhibited sensitivity to X-rays but not to cisplatin. SNM1A was nonepistatic with XRCC3 (homologous recombination), RAD18 (translesion synthesis), FANCC (Fanconi anemia), and SNM1B in ICL repair. SNM1A protein formed punctate nuclear foci depending on the conserved SNM1 (metallo--lactamase) domain. PIAS1 was found to physically interact with SNM1A, and they colocalized at nuclear foci. Point mutations in the SNM1 domain, which disrupted the interaction with PIAS1, led to mislocalization of SNM1A in the nucleus and loss of complementation of snm1a cells. These results suggest that interaction between SNM1A and PIAS1 is required for ICL repair.