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Protein tyrosine phosphatases in cancer: friends and foes!

David P Labbé1, Serge Hardy, Michel L Tremblay

  • 1Goodman Cancer Research Centre, McGill University, Montréal, Québec, Canada.

Progress in Molecular Biology and Translational Science
|February 21, 2012
PubMed

Insights

Protein tyrosine phosphatases (PTPs) are crucial in cancer signaling, acting as both tumor suppressors and oncoproteins. Understanding their dual roles is key for developing novel cancer therapies targeting PTPs.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Tyrosine phosphorylation regulates critical oncogenic pathways like proliferation and apoptosis.
  • Protein tyrosine phosphatases (PTPs) reverse kinase activity, traditionally viewed as tumor suppressors.
  • However, emerging evidence highlights PTPs' potent oncoprotein roles in cancer.

Purpose of the Study:

  • To provide a historical overview of PTPs, their mechanisms, and modifications.
  • To explore the dual properties of PTPs in cancer.
  • To summarize PTP-regulated signaling pathways in human cancers.

Main Methods:

  • Literature review and synthesis of existing research on PTPs.
  • Analysis of PTP mechanisms of action and posttranslational modifications.
  • Focus on classical (receptor and nonreceptor) and dual-specificity phosphatases.

Main Results:

  • PTPs exhibit context-dependent roles, acting as both tumor suppressors (e.g., PTEN) and oncoproteins.
  • Detailed overview of PTPs' diverse functions in cell proliferation, apoptosis, migration, and invasion.
  • Identification of key PTPs and their regulated signaling pathways in human cancers.

Conclusions:

  • PTPs possess dual properties, contributing to both tumor suppression and oncogenesis.
  • Signaling pathways regulated by PTPs are critical in human cancer.
  • PTPs represent promising therapeutic targets for cancer treatment.

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