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

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.

• Authors: Yanhua Zheng, Zhimin Lu
• Journal: Chinese journal of cancer (Chin J Cancer) Vol. 32 Issue 2 Pg. 75-83 (Feb 2013) ISSN: 1000-467X [Print] England
• PMID: 23237212 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't, Review)

Chemical References

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

Topics

• Cell Adhesion
• Cell Movement
• Focal Adhesion Protein-Tyrosine Kinases (metabolism)
• Humans
• Neoplasms (metabolism, 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)