MST1 functions as a key modulator of neurodegeneration in a mouse model of ALS

  • Jae Keun Lee
    Laboratory of Cell Death and Human Diseases, School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Korea;
  • Jin Hee Shin
    GNT Pharma, Suwon 446-906, Korea;
  • Sang Gil Hwang
    Laboratory of Cell Death and Human Diseases, School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Korea;
  • Byoung Joo Gwag
    GNT Pharma, Suwon 446-906, Korea;
  • Ann C. McKee
    Department of Neurology and Pathology, Boston University School of Medicine and VA Boston Healthcare System, Boston, MA 02130;
  • Junghee Lee
    Department of Neurology and Pathology, Boston University School of Medicine and VA Boston Healthcare System, Boston, MA 02130;
  • Neil W. Kowall
    Department of Neurology and Pathology, Boston University School of Medicine and VA Boston Healthcare System, Boston, MA 02130;
  • Hoon Ryu
    Department of Neurology and Pathology, Boston University School of Medicine and VA Boston Healthcare System, Boston, MA 02130;
  • Dae-Sik Lim
    Department of Biological Sciences, Biomedical Research Center, Korea Advanced Institute of Science and Technology, Daejon 305-701, Korea; and
  • Eui-Ju Choi
    Laboratory of Cell Death and Human Diseases, School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Korea;

書誌事項

公開日
2013-07
DOI
  • 10.1073/pnas.1300894110
公開者
Proceedings of the National Academy of Sciences

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説明

<jats:p>Amyotrophic lateral sclerosis (ALS) is an adult-onset neurodegenerative disorder characterized by loss of motor neurons. Dominant mutations in the gene for superoxide dismutase 1 (SOD1) give rise to familial ALS by an unknown mechanism. Here we show that genetic deficiency of mammalian sterile 20-like kinase 1 (MST1) delays disease onset and extends survival in mice expressing the ALS-associated G93A mutant of human SOD1. SOD1(G93A) induces dissociation of MST1 from a redox protein thioredoxin-1 and promotes MST1 activation in spinal cord neurons in a reactive oxygen species–dependent manner. Moreover, MST1 was found to mediate SOD1(G93A)-induced activation of p38 mitogen-activated protein kinase and caspases as well as impairment of autophagy in spinal cord motoneurons of SOD1(G93A) mice. Our findings implicate MST1 as a key determinant of neurodegeneration in ALS.</jats:p>

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