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

Author: Yanhua ZHENG ¹ ; Zhimin LU
Author Information

1. Brain Tumor Center and Department of Neuro-Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
Publication Type:Journal Article
MeSH: 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
From:Chinese Journal of Cancer 2013;32(2):75-83
CountryChina
Language:English
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.