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Updated: May 31, 2026

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.
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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