Added by | liaudet-coopman |
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Group name | EquipeELC |
Item Type | Journal Article |
Title | Tenascin-X promotes epithelial-to-mesenchymal transition by activating latent TGF-? |
Creator | Alcaraz et al. |
Author | Lindsay B. Alcaraz |
Author | Jean-Yves Exposito |
Author | Nicolas Chuvin |
Author | Roxane M. Pommier |
Author | Caroline Cluzel |
Author | Sylvie Martel |
Author | Stéphanie Sentis |
Author | Laurent Bartholin |
Author | Claire Lethias |
Author | Ulrich Valcourt |
Abstract | Transforming growth factor ? (TGF-?) isoforms are secreted as inactive complexes formed through noncovalent interactions between the bioactive TGF-? entity and its N-terminal latency-associated peptide prodomain. Extracellular activation of the latent TGF-? complex is a crucial step in the regulation of TGF-? 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-? complex in vitro and in vivo, thus regulating the bioavailability of mature TGF-? 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 ?11?1 integrin as a cell surface receptor for TNX and show that this integrin is crucial to elicit FBG-mediated activation of latent TGF-? and subsequent epithelial-to-mesenchymal transition in mammary epithelial cells. |
Publication | The Journal of Cell Biology |
Volume | 205 |
Issue | 3 |
Pages | 409-428 |
Date | May 12, 2014 |
Journal Abbr | J. Cell Biol. |
Language | eng |
DOI | 10.1083/jcb.201308031 |
ISSN | 1540-8140 |
Library Catalog | PubMed |
Extra | PMID: 24821840 PMCID: PMC4018787 |
Tags | Animals, Cattle, Cell Adhesion, Cell Line, Tumor, Epithelial Cells, Epithelial-Mesenchymal Transition, Female, firs, first-last-corresponding, HEK293 Cells, Humans, Integrins, Mammary Glands, Animal, Mammary Glands, Human, Mice, original, Phosphorylation, Protein Binding, Protein Conformation, Protein Interaction Domains and Motifs, Protein Precursors, Receptors, Collagen, Recombinant Proteins, RNA Interference, Signal Transduction, Smad Proteins, Tenascin, Transfection, Transforming Growth Factor beta1 |
Date Added | 2019/05/29 - 13:12:25 |
Date Modified | 2019/05/29 - 13:13:01 |
Notes and Attachments | PubMed entry (Attachment) Texte intégral (Attachment) |