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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2011-07-04

AUTHORS

C H Benes, G Poulogiannis, L C Cantley, S P Soltoff

ABSTRACT

Multiple SRC-family kinases (SFKs) are commonly activated in carcinoma and appear to have a role in metastasis through incompletely understood mechanisms. Recent studies have shown that CDCP1 (CUB (complement C1r/C1s, Uegf, Bmp1) Domain-Containing Protein-1) is a transmembrane protein and an SRC substrate potentially involved in metastasis. Here we show that increased SFK and CDCP1 tyrosine phosphorylation is, surprisingly, associated with a decrease in FAK phosphorylation. This appears to be true in human tumors as shown by our correlation analysis of a mass spectrometric data set of affinity-purified phosphotyrosine peptides obtained from normal and cancer lung tissue samples. Induction of tyrosine phosphorylation of CDCP1 in cell culture, including by a mAb that binds to its extracellular domain, promoted changes in SFK and FAK tyrosine phosphorylation, as well as in PKCTM, a protein known to associate with CDCP1, and these changes are accompanied by increases in adhesion and motility. Thus, signaling events that accompany the CDCP1 tyrosine phosphorylation observed in cell lines and human lung tumors may explain how the CDCP1/SFK complex regulates motility and adhesion. More... »

PAGES

653-663

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/onc.2011.262

DOI

http://dx.doi.org/10.1038/onc.2011.262

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1000420328

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/21725358


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