Tensin3 interaction with talin drives the formation of fibronectin-associated fibrillar adhesions.
| Autor: | Atherton P; Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.; Division of Cell Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands., Konstantinou R; Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK.; sGSK Group, Institute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), Singapore, Singapore., Neo SP; Quantitative Proteomics Group, Institute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), Singapore, Singapore., Wang E; Institute of Integrative Biology, University of Liverpool, Liverpool, UK., Balloi E; Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK., Ptushkina M; Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK., Bennett H; Genome Editing Unit, Faculty of Biology, Medicine and Health, University of Manchester, Manchester, UK., Clark K; Department of Biochemistry, University of Leicester, Leicester, UK., Gunaratne J; Quantitative Proteomics Group, Institute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), Singapore, Singapore., Critchley D; Department of Biochemistry, University of Leicester, Leicester, UK., Barsukov I; Institute of Integrative Biology, University of Liverpool, Liverpool, UK., Manser E; sGSK Group, Institute of Molecular and Cell Biology, A*STAR (Agency for Science, Technology and Research), Singapore, Singapore., Ballestrem C; Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, Manchester, UK. |
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| Jazyk: | angličtina |
| Zdroj: | The Journal of cell biology [J Cell Biol] 2022 Oct 03; Vol. 221 (10). Date of Electronic Publication: 2022 Sep 08. |
| DOI: | 10.1083/jcb.202107022 |
| Abstrakt: | The formation of healthy tissue involves continuous remodeling of the extracellular matrix (ECM). Whilst it is known that this requires integrin-associated cell-ECM adhesion sites (CMAs) and actomyosin-mediated forces, the underlying mechanisms remain unclear. Here, we examine how tensin3 contributes to the formation of fibrillar adhesions (FBs) and fibronectin fibrillogenesis. Using BioID mass spectrometry and a mitochondrial targeting assay, we establish that tensin3 associates with the mechanosensors such as talin and vinculin. We show that the talin R11 rod domain binds directly to a helical motif within the central intrinsically disordered region (IDR) of tensin3, whilst vinculin binds indirectly to tensin3 via talin. Using CRISPR knock-out cells in combination with defined tensin3 mutations, we show (i) that tensin3 is critical for the formation of α5β1-integrin FBs and for fibronectin fibrillogenesis, and (ii) the talin/tensin3 interaction drives this process, with vinculin acting to potentiate it. (© 2022 Atherton et al.) |
| Databáze: | MEDLINE |
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