Journal of Applied Biological Chemistry

The Korean Society for Applied Biological Chemistry (한국응용생명화학회)
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Proteomic Identification of Proteins Interacting with a Dual Specificity Protein Phosphatase, VHZ

  • Kim, Jae-Hoon (Facuity of Biotechnology, College of Applied Life Science, Cheju National University) ;
  • Jeong, Dae-Gwin (Systemic Proteomic Research Center, Korea Research Institute of Bioscience and Biotechnology)
  • Published : 2007.06.30
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Abstract

Identification of Dual-specificity protein phosphatase (DSP) substrates is essential in revealing physiological roles of DSPs. We isolated VHZ-interacting proteins from extracts of 293T cells overexpressing a VHZ (C95S, D65A) mutant known to be substrate- trapping mutant. Analysis of specific proteins bound to VHZ by 2D gel electrophoresis and mass spectroscopy revealed that these proteins contained Chaperonin containing TCP1, Type II phosphatidylinositol phosphate kinase ${\gamma}$, Intraflagellar transport 80 homolog, and Kinesin superfamily protein 1B. VHZ-interacting proteins showed that VHZ is involved in many important cellular signal pathways such as protein folding, molecular transportation, and tumor suppression.

Keywords

References

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