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Updated: Jul 17, 2025

Quantitative Measurement of Invadopodia-mediated Extracellular Matrix Proteolysis in Single and Multicellular Contexts
14:23

Quantitative Measurement of Invadopodia-mediated Extracellular Matrix Proteolysis in Single and Multicellular Contexts

Published on: August 27, 2012

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DAB2IP suppresses invadopodia formation through destabilizing ALK by interacting with USP10 in breast cancer

Qingwen Huang1,2, Rui Zhang1,2, Yun Xia3

  • 1Molecular Medicine Center, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, P.R. China.

Iscience
|September 4, 2023
PubMed

Insights

DAB2IP suppresses breast cancer metastasis by inhibiting invadopodia formation. It reduces anaplastic lymphoma kinase (ALK) stability, preventing Cortactin phosphorylation and tumor cell invasion.

Area of Science:

  • Oncology
  • Cell Biology

Background:

  • Invadopodia are crucial for tumor cell invasion and metastasis.
  • DAB2IP is a known tumor suppressor, but its role in invadopodia is unknown.

Purpose of the Study:

  • To elucidate the mechanism of DAB2IP in suppressing breast cancer invadopodia formation and metastasis.

Main Methods:

  • In vitro and in vivo studies in breast cancer models.
  • Investigated the interaction between DAB2IP, ALK, and USP10.
  • Assessed Cortactin phosphorylation levels.

Main Results:

  • DAB2IP suppresses invadopodia formation and metastasis in breast cancer.
  • DAB2IP downregulates ALK by antagonizing USP10-mediated deubiquitination.
  • Inhibition of ALK reduces Cortactin phosphorylation, preventing invadopodia formation.

Conclusions:

  • DAB2IP inhibits breast cancer metastasis by destabilizing ALK via USP10-dependent deubiquitination.
  • This process suppresses Cortactin phosphorylation and invadopodia formation.
  • DAB2IP represents a potential therapeutic target for breast cancer.
Keywords:
CancerMembrane architectureMolecular interactionOrganizational aspects of cell biology

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