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Regulation of tumor cell migration by protein tyrosine phosphatase (PTP)-proline-, glutamate-, serine-,and threonine-rich sequence (PEST) / 癌症
Chinese Journal of Cancer ; (12): 75-83, 2013.
Article in English | WPRIM | ID: wpr-295829
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.
Subject(s)
Full text: Available Index: WPRIM (Western Pacific) Main subject: Oxidation-Reduction / Pathology / Phosphorylation / Cell Adhesion / Cell Movement / Protein Processing, Post-Translational / Src-Family Kinases / Rho GTP-Binding Proteins / Focal Adhesion Protein-Tyrosine Kinases / Protein Tyrosine Phosphatase, Non-Receptor Type 12 Limits: Humans Language: English Journal: Chinese Journal of Cancer Year: 2013 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Oxidation-Reduction / Pathology / Phosphorylation / Cell Adhesion / Cell Movement / Protein Processing, Post-Translational / Src-Family Kinases / Rho GTP-Binding Proteins / Focal Adhesion Protein-Tyrosine Kinases / Protein Tyrosine Phosphatase, Non-Receptor Type 12 Limits: Humans Language: English Journal: Chinese Journal of Cancer Year: 2013 Type: Article