Chie Matsuda

Summary

Affiliation: National Institute of Advanced Industrial Science and Technology
Country: Japan

Publications

  1. ncbi The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle
    C Matsuda
    Molecular Neurobiology Group, Neuroscience Research Institute, AIST, Central 6, Tsukuba 305 8566, Japan
    Hum Mol Genet 10:1761-6. 2001
  2. ncbi Dysferlin interacts with affixin (beta-parvin) at the sarcolemma
    Chie Matsuda
    Research Institute of Neurobiology, Neuroscience Research Institute, AIST, Central 6, Tsukuba, Ibaraki, Japan
    J Neuropathol Exp Neurol 64:334-40. 2005
  3. doi Affixin activates Rac1 via betaPIX in C2C12 myoblast
    Chie Matsuda
    Neuroscience Research Institute, AIST, Central 6, 1 1 1 Higashi, Tsukuba, Ibaraki 305 8566, Japan
    FEBS Lett 582:1189-96. 2008
  4. ncbi The gamma-parvin-integrin-linked kinase complex is critically involved in leukocyte-substrate interaction
    Ryusuke Yoshimi
    Department of Internal Medicine and Clinical Immunology, Yokohama City Graduate School of Medicine, 3 9 Fuku ura, Kanazawa Ku, Yokohama 236 0004, Japan
    J Immunol 176:3611-24. 2006
  5. ncbi Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: ubiquitin/proteasome ERAD(I) and autophagy/lysosome ERAD(II)
    Eriko Fujita
    Divisions of Development and Differentiation, Department of Human Inherited Metabolic Disease, Yokohama, Kanagawa, Japan
    Hum Mol Genet 16:618-29. 2007
  6. pmc Targeted mutation of mouse skeletal muscle sodium channel produces myotonia and potassium-sensitive weakness
    Lawrence J Hayward
    Department of Neurology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA
    J Clin Invest 118:1437-49. 2008

Collaborators

  • I Nishino
  • Y K Hayashi
  • I Nonaka
  • Eric Hoffman
  • Lawrence J Hayward
  • Eriko Fujita
  • Ryusuke Yoshimi
  • Joanna S Kim
  • Ming Yang Lee
  • Jean Marc Renaud
  • Kumudini Misra
  • Didier Cros
  • Ji W Kim
  • Hongru Zhou
  • Robert H Brown
  • Valerie Reid
  • Mohammad Salajegheh
  • Fen fen Wu
  • Stephen C Cannon
  • Hiromichi Kumagai
  • Akifumi Misutani
  • Yoriko Kouroku
  • Takashi Momoi
  • Atsushi Isoai
  • Satoshi Yamaji
  • Mayumi Okamura
  • Yoshihiro Miwa
  • Shigeo Ohno
  • Atsushi Suzuki
  • Wataru Mishima
  • Takashi Obana
  • Yoshiaki Ishigatsubo

Detail Information

Publications6

  1. ncbi The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle
    C Matsuda
    Molecular Neurobiology Group, Neuroscience Research Institute, AIST, Central 6, Tsukuba 305 8566, Japan
    Hum Mol Genet 10:1761-6. 2001
    ..This is the first description of a possible dysferlin interacting protein; it suggests the hypothesis that one function of dysferlin may be to interact with caveolin-3 to subserve signaling functions of caveolae...
  2. ncbi Dysferlin interacts with affixin (beta-parvin) at the sarcolemma
    Chie Matsuda
    Research Institute of Neurobiology, Neuroscience Research Institute, AIST, Central 6, Tsukuba, Ibaraki, Japan
    J Neuropathol Exp Neurol 64:334-40. 2005
    ..We also found N-terminal calponin homology domain of affixin as a binding site for dysferlin. Our results suggest that affixin may participate in membrane repair with dysferlin...
  3. doi Affixin activates Rac1 via betaPIX in C2C12 myoblast
    Chie Matsuda
    Neuroscience Research Institute, AIST, Central 6, 1 1 1 Higashi, Tsukuba, Ibaraki 305 8566, Japan
    FEBS Lett 582:1189-96. 2008
    ..These results suggest that affixin is involved in reorganization of subsarcolemmal cytoskeletal actin by activation of Rac1 through alpha and betaPIXs in skeletal muscle...
  4. ncbi The gamma-parvin-integrin-linked kinase complex is critically involved in leukocyte-substrate interaction
    Ryusuke Yoshimi
    Department of Internal Medicine and Clinical Immunology, Yokohama City Graduate School of Medicine, 3 9 Fuku ura, Kanazawa Ku, Yokohama 236 0004, Japan
    J Immunol 176:3611-24. 2006
    ....
  5. ncbi Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: ubiquitin/proteasome ERAD(I) and autophagy/lysosome ERAD(II)
    Eriko Fujita
    Divisions of Development and Differentiation, Department of Human Inherited Metabolic Disease, Yokohama, Kanagawa, Japan
    Hum Mol Genet 16:618-29. 2007
    ..Mutant dysferlin aggregates on the ER are degraded by the autophagy/lysosome ERAD(II), as an alternative to ERAD(I), when retrotranslocon/ERAD(I) system is impaired by these mutant aggregates...
  6. pmc Targeted mutation of mouse skeletal muscle sodium channel produces myotonia and potassium-sensitive weakness
    Lawrence J Hayward
    Department of Neurology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA
    J Clin Invest 118:1437-49. 2008
    ....