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Role of Shp2 Tyrosine Phosphatase in Trophic Effects of BDNF in Cultured Dopaminergic Neurons of Substantia Nigra

  • Satomi Takai
  • Toshiyuki Araki
  • Hisatsugu Koshimizu
  • Hiroshi Hatanaka
  • Masashi Yamada
Part of the Advances in Behavioral Biology book series (ABBI, volume 53)

Abstract

Brain-derived neurotrophic factor (BDNF), a member of the neurotrophin family, works as a neurotrophic factor, promoting differentiation and survival in a variety of CNS neurons.1,5 BDNF binds to a receptor tyrosine kinase, TrkB, a member of the Trk family, to exert its effects. Shp2, a protein tyrosine phosphatase, is activated by various growth factors, and is activated by association with tyrosine-phosphorylated proteins via its two SH2 domains. Studies using phosphatase-inactive and phosphatase domain deficient mutants of Shp2 suggested that Shp2 functions as a positive regulator of MAPK activation and proliferation in various types of mitogenic cells. Shp2 is highly expressed in the brain. Recently, we observed that Shp2 is involved in BDNF signaling in cultured cerebral cortical neurons.2,7 However, it is not clearly understood how Shp2 functions in response to BDNF in neurons.

Keywords

BDNF Signaling Cerebral Cortical Neuron Mesencephalic Neuron Mesencephalic Dopaminergic Neuron BDNF Signaling Pathway 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 2002

Authors and Affiliations

  • Satomi Takai
  • Toshiyuki Araki
  • Hisatsugu Koshimizu
  • Hiroshi Hatanaka
  • Masashi Yamada
    • 1
  1. 1.Division of Protein Biosynthesis, Institute for Protein ResearchOsaka UniversitySuita, OsakaJapan

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