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Related Experiment Video

Updated: Jul 9, 2026

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors
08:45

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Published on: July 17, 2020

New insights into PTEN.

Tanja Tamguney1, David Stokoe

  • 1UCSF Cancer Research Institute, 2340 Sutter Street, San Francisco, CA 94115, USA.

Journal of Cell Science
|November 23, 2007
PubMed
Summary
This summary is machine-generated.

PTEN (phosphatase and tensin homolog) is a tumor suppressor with diverse functions beyond dephosphorylation. Its complex regulation and subcellular localization are critical for normal cellular processes and implicated in diseases like cancer, diabetes, and autism.

Related Experiment Videos

Last Updated: Jul 9, 2026

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors
08:45

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Published on: July 17, 2020

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • PTEN (phosphatase and tensin homolog) was initially identified as a tumor suppressor gene frequently mutated in human cancers.
  • Its known functions extend beyond lipid and protein dephosphorylation, encompassing phosphatase-independent activities.
  • PTEN's cellular roles are intricate, involving complex regulatory mechanisms and dynamic subcellular localization.

Purpose of the Study:

  • To provide a comprehensive overview of PTEN's multifaceted functions.
  • To elucidate the complex regulatory networks governing PTEN activity.
  • To highlight PTEN's involvement in both cancerous and non-cancerous human diseases.

Main Methods:

  • Literature review and synthesis of existing research on PTEN.
  • Analysis of PTEN's biochemical activities, including phosphatase-dependent and -independent functions.
  • Examination of PTEN's transcriptional and post-translational regulation (phosphorylation, ubiquitylation, oxidation, acetylation).
  • Investigation of PTEN's subcellular localization (plasma membrane, cytoplasm, nucleus) and its implications.

Main Results:

  • PTEN exhibits diverse functions, including lipid and protein dephosphorylation, as well as phosphatase-independent activities.
  • PTEN function is tightly regulated at both transcriptional and post-translational levels.
  • PTEN's subcellular distribution is dynamic and crucial for its diverse roles.
  • Dysregulation of PTEN is implicated in a spectrum of diseases, including cancer, diabetes, and autism.

Conclusions:

  • PTEN is a critical regulator with a broader functional repertoire than previously understood.
  • Understanding PTEN's complex regulation and localization is key to deciphering its role in health and disease.
  • Targeting PTEN pathways holds potential for therapeutic interventions in various human pathologies.