TβRIII/β-arrestin2 regulates integrin α5β1 trafficking, function, and localization in epithelial cells
The type III TGF-β receptor (TβRIII) is a ubiquitous co-receptor for TGF-β superfamily ligands with roles in suppressing cancer progression, in part through suppressing cell motility. Here we demonstrate that TβRIII promotes epithelial cell adhesion to fibronectin in a β-arrestin2 dependent and TGF-...
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| Veröffentlicht in: | Oncogene 2013-03, Vol.32 (11), p.1416-1427 |
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| creator | Mythreye, K Knelson, E H Gatza, C E Gatza, M L Blobe, G C |
| description | The type III TGF-β receptor (TβRIII) is a ubiquitous co-receptor for TGF-β superfamily ligands with roles in suppressing cancer progression, in part through suppressing cell motility. Here we demonstrate that TβRIII promotes epithelial cell adhesion to fibronectin in a β-arrestin2 dependent and TGF-β/BMP independent manner by complexing with active integrin α5β1, and mediating β-arrestin2-dependent α5β1 internalization and trafficking to nascent focal adhesions. TβRIII-mediated integrin α5β1 trafficking regulates cell adhesion and fibronectin fibrillogenesis in epithelial cells, as well as α5 localization in breast cancer patients. We further demonstrate that increased TβRIII expression correlates with increased α5 localization at sites of cell-cell adhesion in breast cancer patients, while higher TβRIII expression is a strong predictor of overall survival in breast cancer patients. These data support a novel, clinically relevant role for TβRIII in regulating integrin α5 localization, reveal a novel crosstalk mechanism between the integrin and TGF-β superfamily signaling pathways and identify β-arrestin2 as a regulator of α5β1 trafficking. |
| doi_str_mv | 10.1038/onc.2012.157 |
| format | Article |
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Here we demonstrate that TβRIII promotes epithelial cell adhesion to fibronectin in a β-arrestin2 dependent and TGF-β/BMP independent manner by complexing with active integrin α5β1, and mediating β-arrestin2-dependent α5β1 internalization and trafficking to nascent focal adhesions. TβRIII-mediated integrin α5β1 trafficking regulates cell adhesion and fibronectin fibrillogenesis in epithelial cells, as well as α5 localization in breast cancer patients. We further demonstrate that increased TβRIII expression correlates with increased α5 localization at sites of cell-cell adhesion in breast cancer patients, while higher TβRIII expression is a strong predictor of overall survival in breast cancer patients. 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Here we demonstrate that TβRIII promotes epithelial cell adhesion to fibronectin in a β-arrestin2 dependent and TGF-β/BMP independent manner by complexing with active integrin α5β1, and mediating β-arrestin2-dependent α5β1 internalization and trafficking to nascent focal adhesions. TβRIII-mediated integrin α5β1 trafficking regulates cell adhesion and fibronectin fibrillogenesis in epithelial cells, as well as α5 localization in breast cancer patients. We further demonstrate that increased TβRIII expression correlates with increased α5 localization at sites of cell-cell adhesion in breast cancer patients, while higher TβRIII expression is a strong predictor of overall survival in breast cancer patients. These data support a novel, clinically relevant role for TβRIII in regulating integrin α5 localization, reveal a novel crosstalk mechanism between the integrin and TGF-β superfamily signaling pathways and identify β-arrestin2 as a regulator of α5β1 trafficking.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>22562249</pmid><doi>10.1038/onc.2012.157</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/67/1347 631/80/313 631/80/79/1236 631/80/86 Animals Apoptosis Arrestins - genetics Arrestins - metabolism Arrestins - physiology beta-Arrestins Breast cancer Caco-2 Cells Cell adhesion Cell adhesion & migration Cell Adhesion - genetics Cell Biology Cells, Cultured Epithelial cells Epithelial Cells - metabolism Fibrillogenesis Fibronectin Fibronectins - metabolism Human Genetics Humans Integrin alpha5beta1 - metabolism Integrin alpha5beta1 - physiology Internal Medicine Internalization K562 Cells Localization Medicine Medicine & Public Health Mice Models, Biological Oncology original-article Protein Interaction Domains and Motifs - physiology Protein Transport - genetics Proteoglycans - chemistry Proteoglycans - genetics Proteoglycans - metabolism Proteoglycans - physiology Receptors, Transforming Growth Factor beta - chemistry Receptors, Transforming Growth Factor beta - genetics Receptors, Transforming Growth Factor beta - metabolism Receptors, Transforming Growth Factor beta - physiology Tissue Distribution - genetics Transforming growth factor-b |
| title | TβRIII/β-arrestin2 regulates integrin α5β1 trafficking, function, and localization in epithelial cells |
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