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Related Experiment Video

Updated: Jul 2, 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

HD-PTP inhibits endothelial migration through its interaction with Src.

Massimo Mariotti1, Sara Castiglioni, Jose M Garcia-Manteiga

  • 1Department of Preclinical Sciences, University of Milan Medical School, Via GB Grassi 74, Milan, Italy. jeanette.maier@unimi.it

The International Journal of Biochemistry & Cell Biology
|September 3, 2008
PubMed
Summary

The tyrosine phosphatase HD-PTP regulates endothelial cell migration. Its activity is inhibited by Src phosphorylation, revealing a novel mechanism in angiogenesis and cell motility.

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Last Updated: Jul 2, 2026

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

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Methods to Study Mrp4-containing Macromolecular Complexes in the Regulation of Fibroblast Migration
10:43

Methods to Study Mrp4-containing Macromolecular Complexes in the Regulation of Fibroblast Migration

Published on: May 19, 2016

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Endothelial migration is crucial for angiogenesis and regulated by tyrosine kinases and phosphatases.
  • HD-PTP (Hic-5/Daughter of Hic-5) is implicated in endothelial motility, with its silencing leading to altered cell morphology and increased migration.
  • The proto-oncogene Src is known to regulate cell motility, and HD-PTP has a potential binding site for Src.

Purpose of the Study:

  • To investigate the interplay between HD-PTP and Src in the context of endothelial cell migration.
  • To determine if Src phosphorylates HD-PTP and how this affects HD-PTP's enzymatic activity.
  • To elucidate the role of the HD-PTP/Src interaction in endothelial motility.

Main Methods:

  • Co-immunoprecipitation assays to detect binding between Src and HD-PTP.
  • In vitro and in vivo phosphorylation assays to assess Src's effect on HD-PTP.
  • Enzymatic assays to measure HD-PTP tyrosine phosphatase activity.
  • Pharmacological and genetic inhibition of Src in endothelial cells with silenced HD-PTP.
  • Analysis of endothelial cell morphology and migration patterns.

Main Results:

  • Src binds to HD-PTP, with enhanced interaction upon basic fibroblast growth factor exposure.
  • Src phosphorylates HD-PTP on tyrosine residues, which inhibits HD-PTP's tyrosine phosphatase activity.
  • HD-PTP possesses intrinsic tyrosine phosphatase activity.
  • Inhibition of Src abrogates the enhanced migratory phenotype observed in HD-PTP-silenced endothelial cells.
  • HD-PTP was previously shown to bind and dephosphorylate FAK, another regulator of cell migration.

Conclusions:

  • HD-PTP functions as a tyrosine phosphatase regulating endothelial cell motility.
  • Src-mediated phosphorylation of HD-PTP inhibits its phosphatase activity, suggesting a regulatory mechanism.
  • The interaction between HD-PTP and Src is critical for controlling endothelial cell migration.
  • HD-PTP likely regulates endothelial motility through coordinated interactions with both Src and FAK.