Skip Navigation



Carcinogenesis Advance Access published online on September 7, 2009
Carcinogenesis, doi:10.1093/carcin/bgp217
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow Supplementary Data
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Romero, D.
Right arrow Articles by Vary, C. P.H.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Romero, D.
Right arrow Articles by Vary, C. P.H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2009. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

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

Diana Romero, Aleksandra Terzic, Barbara A. Conley, Clarissa Craft{int}, Borko Jovanovic§, Raymond Bergan and Calvin P.H. Vary§

Center for Molecular Medicine, Maine Medical Center Research Institute, Scarborough, ME 04074, USA
{int} Department of Cell Biology & Physiology, Washington University Medical School, St. Louis, MO 63110, USA
§ Department of Preventive Medicine, Northwestern University, Chicago, IL 60611, USA
Division of Hematology/Oncology, Department of Medicine, Northwestern University Medical School, and the Robert H. Lurie Cancer Center of Northwestern University, Chicago, IL 60611, USA

Address correspondence to: Calvin P.H. Vary, Maine Medical Center Research Institute, 81 Research Drive, Scarborough, ME 04074, Tel. (207) 885-8148; Fax (207) 885-8179; Email: varyc{at}mmc.org

Endoglin, a transmembrane glycoprotein that acts as a transforming growth factor beta coreceptor, is down-regulated 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.

Key Words: transforming growth factor beta • bone morphogenetic protein • PC3-M • endoglin • ALK2

Received March 17, 2009; revised August 26, 2009; accepted August 29, 2009.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.