Regulation of tumor cell migration by protein tyrosine phosphatase (PTP)-proline-, glutamate-, serine-,and threonine-rich sequence (PEST)

Chin J Cancer. 2013 Feb;32(2):75-83. doi: 10.5732/cjc.012.10084. Epub 2012 Dec 7.

Abstract

Protein tyrosine phosphatase (PTP)-proline-, glutamate-, serine-, and threonine-rich sequence (PEST) is ubiquitously expressed and is a critical regulator of cell adhesion and migration. PTP-PEST activity can be regulated transcriptionally via gene deletion or mutation in several types of human cancers or via post-translational modifications, including phosphorylation, oxidation, and caspase-dependent cleavage. PTP-PEST interacts with and dephosphorylates cytoskeletal and focal adhesion-associated proteins. Dephosphorylation of PTP-PEST substrates regulates their enzymatic activities and/or their interaction with other proteins and plays an essential role in the tumor cell migration process.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cell Adhesion
  • Cell Movement*
  • Focal Adhesion Protein-Tyrosine Kinases / metabolism
  • Humans
  • Neoplasms / metabolism
  • Neoplasms / pathology*
  • Oxidation-Reduction
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Protein Tyrosine Phosphatase, Non-Receptor Type 12 / metabolism*
  • Shc Signaling Adaptor Proteins / metabolism
  • rho GTP-Binding Proteins / metabolism
  • src-Family Kinases / metabolism

Substances

  • Shc Signaling Adaptor Proteins
  • Focal Adhesion Protein-Tyrosine Kinases
  • src-Family Kinases
  • Protein Tyrosine Phosphatase, Non-Receptor Type 12
  • rho GTP-Binding Proteins