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Updated: May 23, 2026

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

Published on: July 17, 2020

Shp2 function in hematopoietic stem cell biology and leukemogenesis.

Sarah C Nabinger¹, Rebecca J Chan

¹Department of Pediatrics, Herman B Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, Indiana, USA.

Current Opinion in Hematology

|April 17, 2012

Summary

Shp2 protein is crucial for normal blood cell development. Its mutations drive Noonan syndrome and leukemia, with specific mutations causing distinct effects on hematopoietic stem cells and disease progression.

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Assessing Cellular Target Engagement by SHP2 (PTPN11) Phosphatase Inhibitors

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Retroviral Infection of Murine Embryonic Stem Cell Derived Embryoid Body Cells for Analysis of Hematopoietic Differentiation

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Published on: October 20, 2014

Area of Science:

Hematology
Molecular Biology
Cancer Research

Background:

The protein tyrosine phosphatase Shp2, encoded by PTPN11, plays a vital role in regulating normal blood cell formation (hematopoiesis).
Mutations in PTPN11 are linked to Noonan syndrome and contribute to the development of human leukemias.
Animal models are essential for studying Shp2's function in hematopoietic stem cells (HSCs) and its role in leukemic transformation.

Purpose of the Study:

To investigate the necessity of Shp2 in HSC function and repopulating capacity using animal models.
To examine the distinct effects of different PTPN11 mutations on HSCs and leukemogenesis.
To understand the mechanisms underlying Shp2's role in both normal hematopoiesis and pathological conditions.

Main Methods:

Generation and analysis of independent animal models with Shp2 knockout in hematopoietic tissues.
In vivo studies of HSC quiescence, apoptosis, and repopulating capacity.
Transplantation experiments using HSCs with specific Shp2 mutations (Shp2D61G, Shp2D61Y, Shp2E76K) to assess their impact on myeloproliferative disease (MPD) and leukemia development.

Main Results:

Shp2 is essential for HSC repopulating capacity; its absence leads to reduced quiescence and increased apoptosis.
The germline mutation Shp2D61G enhances HSC activity and induces MPD.
Somatic mutations Shp2D61Y and Shp2E76K induce MPD, with Shp2E76K additionally promoting transformation to acute leukemia, demonstrating distinct pathogenic potentials.

Conclusions:

Shp2 is critical for maintaining HSC function and preventing leukemic transformation.
Specific PTPN11 mutations confer unique oncogenic properties, influencing MPD and acute leukemia development.
Further research into Shp2's dual role in physiology and pathology is crucial for developing targeted therapies for Shp2-associated diseases.