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 FNR01 image overlay with phase contrast background. Fluorescent fibronectin (Cat. # FNR01) treated MCF10A cells (image kindly provided by A. Varadara and M. Karthykenyan, Univ. S.Carolina, Columbia, SC).
FNR01 image overlay with phase contrast background. Fluorescent fibronectin (Cat. # FNR01) treated MCF10A cells (image kindly provided by A. Varadara and M. Karthykenyan, Univ. S.Carolina, Columbia, SC).

Recently, Varadaraj et al. examined transforming growth factor β (TGF-β) regulation of the extracellular matrix (ECM) protein fibronectin (FN). Soluble FN dimers polymerize to form insoluble, matrix-associated FN polymers in a process known as fibrillogenesis. The resulting FN fibril network is a scaffold for cell migration, repair, and adhesion mediated by binding to α5β1 integrin receptors. TGF-β stimulates ECM remodeling and cell migration through the induction of FN fibrillogenesis, which is necessary for TGF-β’s effects. Here, the authors found that FN’s role in TGF-β-mediated ECM remodeling and cell migration can occur via increased FN trafficking, i.e., recycling between the plasma membrane and cytosol. In response to TGF-β, cell surface FN is endocytosed and undergoes Rab11-mediated recycling and subsequent incorporation into fibrils, a process dependent on an interaction between the cytoplasmic domain of the type II TGF-β receptor (TβRII) and a5b1 integrin. Cytoskeleton’s rhodamine-labeled and biotinylated fibronectin (Cat. # FNR01 and  FNR03 respectively) were essential reagents in this interesting study, providing the tools necessary to discover that TGF-β induces FN trafficking/recycling, a novel process that offers a rapid pathway by which FN can regulate cell migration, wound repair, and fibrosis.

 

Link to citation: 

Varadaraj A. et al. 2017. TGF-β triggers rapid fibrillogenesis via a novel TβRII dependent fibronectin trafficking mechanism. Mol. Biol. Cell. DOI: 10.1091/mbc.E16-08-0601.

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alex castellanos