Shp-2 regulates the TrkB receptor activity in the retinal ganglion cells under glaucomatous stress

Biochim Biophys Acta. 2012 Nov;1822(11):1643-9. doi: 10.1016/j.bbadis.2012.07.016. Epub 2012 Aug 3.

Abstract

Tropomyosin-receptor-kinase B (TrkB receptor) activation plays an important role in the survival of retinal ganglion cells (RGCs). This study reports a novel finding that, SH2 domain-containing phosphatase-2 (Shp-2) binds to the TrkB receptor in RGCs and negatively regulates its activity under glaucomatous stress. This enhanced binding of TrkB and Shp2 is mediated through caveolin. Caveolin 1 and 3 undergo hyper-phosphorylation in RGCs under stress and bind to the Shp2 phosphatase. Shp2 undergoes activation under glaucomatous stress conditions in RGCs in vivo with a concurrent loss of TrkB activity. Inhibiting the Shp2 phosphatase restored TrkB activity in cells exposed to excitotoxic and oxidative stress. Collectively, these findings implicate a molecular basis of Shp2 mediated TrkB deactivation leading to RGC degeneration observed in glaucoma.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Caveolin 1 / metabolism
  • Caveolin 3 / metabolism
  • Cell Survival
  • Cells, Cultured
  • Glaucoma / metabolism*
  • Oligodeoxyribonucleotides, Antisense
  • Optic Nerve Injuries
  • Oxidative Stress
  • Phosphorylation
  • Protein Tyrosine Phosphatase, Non-Receptor Type 11 / metabolism*
  • Rats
  • Rats, Sprague-Dawley
  • Receptor, trkB / metabolism*
  • Retinal Ganglion Cells / metabolism*
  • Retinal Ganglion Cells / pathology
  • Signal Transduction
  • src Homology Domains

Substances

  • Cav3 protein, rat
  • Caveolin 1
  • Caveolin 3
  • Oligodeoxyribonucleotides, Antisense
  • Receptor, trkB
  • Protein Tyrosine Phosphatase, Non-Receptor Type 11