Journal Article

Endoglin phosphorylation by ALK2 contributes to the regulation of prostate cancer cell migration

Diana Romero, Aleksandra Terzic, Barbara A. Conley, Clarissa S. Craft, Borko Jovanovic, Raymond C. Bergan and Calvin P.H. Vary

in Carcinogenesis

Volume 31, issue 3, pages 359-366
Published in print March 2010 | ISSN: 0143-3334
Published online September 2009 | e-ISSN: 1460-2180 | DOI: http://dx.doi.org/10.1093/carcin/bgp217
Endoglin phosphorylation by ALK2 contributes to the regulation of prostate cancer cell migration

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Endoglin, a transmembrane glycoprotein that acts as a transforming growth factor-β (TGF-β) coreceptor, is downregulated in PC3-M metastatic prostate cancer cells. When restored, endoglin expression in PC3-M cells inhibits cell migration in vitro and attenuates the tumorigenicity of PC3-M cells in SCID mice, though the mechanism of endoglin regulation of migration in prostate cancer cells is not known. The current study indicates that endoglin is phosphorylated on cytosolic domain threonine residues by the TGF-β type I receptors ALK2 and ALK5 in prostate cancer cells. Importantly, in the presence of constitutively active ALK2, endoglin did not inhibit cell migration, suggesting that endoglin phosphorylation regulated PC3-M cell migration. Therefore, our results suggest that endoglin phosphorylation is a mechanism with relevant functional consequences in prostate cancer cells. These data demonstrate for the first time that TGF-β receptor-mediated phosphorylation of endoglin is a Smad-independent mechanism involved in the regulation of prostate cancer cell migration.

Journal Article.  4867 words.  Illustrated.

Subjects: Clinical Cytogenetics and Molecular Genetics

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