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Updated: May 31, 2026

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

The SRC-associated protein CUB Domain-Containing Protein-1 regulates adhesion and motility

C H Benes1, G Poulogiannis, L C Cantley

  • 1Department of Medicine, Division of Signal Transduction, Beth Israel Deaconess Medical Center, Boston, MA 02215, USA.

Oncogene
|July 5, 2011
PubMed

Insights

Increased tyrosine phosphorylation of CDCP1 (CUB Domain-Containing Protein-1) and SRC-family kinases (SFKs) correlates with decreased FAK phosphorylation in lung tumors. This suggests a novel mechanism for CDCP1/SFK in regulating cell adhesion and motility during metastasis.

Area of Science:

  • Oncology
  • Molecular Biology
  • Cell Biology

Background:

  • SRC-family kinases (SFKs) are frequently activated in carcinomas, implicating them in metastasis via poorly understood pathways.
  • CDCP1 (CUB Domain-Containing Protein-1) is a transmembrane protein and SFK substrate potentially involved in cancer metastasis.

Purpose of the Study:

  • To investigate the relationship between CDCP1, SFKs, and FAK phosphorylation in carcinoma.
  • To elucidate the role of CDCP1 phosphorylation in regulating cell adhesion and motility.

Main Methods:

  • Correlation analysis of phosphotyrosine peptide mass spectrometry data from human lung tumors.
  • Induction of CDCP1 tyrosine phosphorylation in cell culture using a monoclonal antibody (mAb).
  • Analysis of SFK, FAK, and PKC(TM) phosphorylation, cell adhesion, and motility.

Main Results:

  • Increased SFK and CDCP1 tyrosine phosphorylation was surprisingly associated with decreased FAK phosphorylation in human lung tumors.
  • CDCP1 tyrosine phosphorylation in cell culture altered SFK and FAK phosphorylation patterns.
  • These signaling changes were accompanied by increased cell adhesion and motility.

Conclusions:

  • CDCP1 tyrosine phosphorylation, influenced by SFKs, plays a role in regulating cell adhesion and motility.
  • The CDCP1/SFK complex signaling pathway offers potential therapeutic targets for inhibiting metastasis in carcinoma.

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