Atherton, Paul, Konstantinou, Rafaella, Neo, Suat Peng, Wang, Emily, Balloi, Eleonora, Ptushkina, Marina, Bennett, Hayley, Clark, Kath, Gunaratne, Jayantha, Critchley, David et al (show 3 more authors)
(2022)
Tensin3 interaction with talin drives the formation of fibronectin-associated fibrillar adhesions.
JOURNAL OF CELL BIOLOGY, 221 (10).
e202107022-.
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Abstract
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.
Item Type: | Article |
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Uncontrolled Keywords: | Focal Adhesions, Extracellular Matrix, Talin, Vinculin, Fibronectins, Integrins, Cell Adhesion, Tensins |
Divisions: | Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology |
Depositing User: | Symplectic Admin |
Date Deposited: | 03 Mar 2023 11:46 |
Last Modified: | 08 Mar 2023 16:23 |
DOI: | 10.1083/jcb.202107022 |
Related URLs: | |
URI: | https://livrepository.liverpool.ac.uk/id/eprint/3168735 |