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.
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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