| First Author | Alcaraz LB | Year | 2014 |
| Journal | J Cell Biol | Volume | 205 |
| Issue | 3 | Pages | 409-28 |
| PubMed ID | 24821840 | Mgi Jnum | J:215800 |
| Mgi Id | MGI:5606260 | Doi | 10.1083/jcb.201308031 |
| Citation | Alcaraz LB, et al. (2014) Tenascin-X promotes epithelial-to-mesenchymal transition by activating latent TGF-beta. J Cell Biol 205(3):409-28 |
| abstractText | Transforming growth factor beta (TGF-beta) isoforms are secreted as inactive complexes formed through noncovalent interactions between the bioactive TGF-beta entity and its N-terminal latency-associated peptide prodomain. Extracellular activation of the latent TGF-beta complex is a crucial step in the regulation of TGF-beta function for tissue homeostasis. We show that the fibrinogen-like (FBG) domain of the matrix glycoprotein tenascin-X (TNX) interacts physically with the small latent TGF-beta complex in vitro and in vivo, thus regulating the bioavailability of mature TGF-beta to cells by activating the latent cytokine into an active molecule. Activation by the FBG domain most likely occurs through a conformational change in the latent complex and involves a novel cell adhesion-dependent mechanism. We identify alpha11beta1 integrin as a cell surface receptor for TNX and show that this integrin is crucial to elicit FBG-mediated activation of latent TGF-beta and subsequent epithelial-to-mesenchymal transition in mammary epithelial cells. |
