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Updated: Jul 13, 2026

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors
Published on: July 17, 2020
PP2A: unveiling a reluctant tumor suppressor
1Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. marc.mumby@utsouthwestern.edu
Abstract:
Although evidence has suggested that the serine/threonine protein phosphatase 2A (PP2A) might be a tumor suppressor protein, it has been difficult to pin down its role in tumor suppression because it acts in a wide variety of signaling pathways. Recent findings, including work in this issue by Junttila et al. (2007), provide convincing evidence that suppression of PP2A activity cooperates with other oncogenic changes to cause transformation of multiple cell types.
Insights
Serine/threonine protein phosphatase 2A (PP2A) may act as a tumor suppressor. New evidence shows that reduced PP2A activity collaborates with other cancer-driving changes to transform cells.
Area of Science:
- Molecular Biology
- Oncology
- Biochemistry
Background:
- The serine/threonine protein phosphatase 2A (PP2A) has been implicated as a potential tumor suppressor.
- Its precise role in tumor suppression is complex due to its involvement in numerous signaling pathways.
Discussion:
- Recent findings demonstrate that the suppression of PP2A activity cooperates with other oncogenic alterations.
- This cooperation leads to the transformation of various cell types, highlighting PP2A's critical function.
Key Insights:
- PP2A's tumor suppressor role is supported by evidence showing its activity is crucial for preventing cellular transformation.
- Loss of PP2A function, in conjunction with other oncogenic events, is sufficient to drive malignant progression.
Outlook:
- Further research into PP2A signaling pathways could reveal new therapeutic targets for cancer treatment.
- Understanding how PP2A interacts with other oncogenes is vital for developing effective anti-cancer strategies.
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