CDCP1/Trask is a 140 kD transmembrane glycoprotein with a large extracellular domain (ECD) containing two CUB domains, and a smaller intracellular domain (ICD) containing five tyrosines. The tyrosine phosphorylation of Trask is tightly regulated and reciprocally linked with the state of cell adhesion. The tyrosine phosphorylation of CDCP1 in cultured cells occurs when cells are induced to detach by trypsin or EDTA, or seen spontaneously during mitotic detachment. The overexpression of CDCP1 leads to the loss of cell adhesion and a detached phenotype. CDCP1 is widely expressed in human epithelial tissues, but its phosphorylation is only seen in mitotically detached or shedding cells, consistent with its role in the negative regulation of cell adhesion.
The phosphorylation of CDCP1 is seen in many cancers, including some pre-invasive cancers as well as in invasive tumors and in tumor metastases. The functional implications of CDCP1 phosphorylation in tumors is currently under investigation.
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