title: Protein tyrosine phosphatases in cancer: friends and foes!
abstract: Tyrosine phosphorylation of proteins serves as an exquisite switch in controlling several key oncogenic signaling pathways involved in cell proliferation, apoptosis, migration, and invasion. Since protein tyrosine phosphatases (PTPs) counteract protein kinases by removing phosphate moieties on target proteins, one may intuitively think that PTPs would act as tumor suppressors. Indeed, one of the most described PTPs, namely, the phosphatase and tensin homolog (PTEN), is a tumor suppressor. However, a growing body of evidence suggests that PTPs can also function as potent oncoproteins. In this chapter, we provide a broad historical overview of the PTPs, their mechanism of action, and posttranslational modifications. Then, we focus on the dual properties of classical PTPs (receptor and nonreceptor) and dual-specificity phosphatases in cancer and summarize the current knowledge of the signaling pathways regulated by key PTPs in human cancer. In conclusion, we present our perspective on the potential of these PTPs to serve as therapeutic targets in cancer.
authors.affiliation: Goodman Cancer Research Centre, McGill University, Montréal, Québec, Canada.
authors.forename: David P
authors.initials: DP
authors.lastname: Labbé
authors.forename: Serge
authors.initials: S
authors.lastname: Hardy
authors.forename: Michel L
authors.initials: ML
authors.lastname: Tremblay
mesh_terms: D000494:Allosteric Regulation; D000818:Animals; D000970:Antineoplastic Agents / Q000494:pharmacology / Q000627:therapeutic use; D004791:Enzyme Inhibitors / Q000494:pharmacology / Q000627:therapeutic use; D006801:Humans; D058990:Molecular Targeted Therapy; D009363:Neoplasm Proteins / Q000037:antagonists & inhibitors / Q000502:physiology*; D009369:Neoplasms / Q000188:drug therapy / Q000201:enzymology* / Q000473:pathology; D010084:Oxidation-Reduction; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation / Q000187:drug effects; D019000:Phosphotyrosine / Q000378:metabolism; D054876:Prenylation; D011499:Protein Processing, Post-Translational / Q000187:drug effects / Q000502:physiology; D017027:Protein Tyrosine Phosphatases / Q000037:antagonists & inhibitors / Q000502:physiology*; D011505:Protein-Tyrosine Kinases / Q000502:physiology; D015398:Signal Transduction / Q000187:drug effects / Q000502:physiology; D013329:Structure-Activity Relationship; D058207:Sumoylation; D025521:Tumor Suppressor Proteins / Q000502:physiology
chemical_list: D000970:Antineoplastic Agents; D004791:Enzyme Inhibitors; D009363:Neoplasm Proteins; D010750:Phosphoproteins; D025521:Tumor Suppressor Proteins; D019000:Phosphotyrosine; D011505:Protein-Tyrosine Kinases; D017027:Protein Tyrosine Phosphatases