摘要
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.Dephos-phorylation 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.
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 posttranslational modifications, including phosphorylation, oxidation, and caspase-dependent cleavage. PTPPEST 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.
基金
supported by National Cancer Institute grants 2R01CA109035 (Z.L.) and CA16672(Cancer Center Support Grant)
research grant RP110252 (Z.L.) from the Cancer Prevention and Research Institute of Texas (CPRIT)
American Cancer Society Research Scholar Award RSG-09-277-01-CSM(Z.L.)
the James S. McDonnell Foundation 21st Century Science Initiative in Brain Cancer Research Award(220020318 Z.L.)
a Sister Institution Network Fund from The University of Texas MD Anderson Cancer Center (Z.L.)
