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Tensin3 interaction with talin drives formation of fibronectin-associated fibrillar adhesions

ABSTRACT: The formation of healthy tissue involves continuous remodelling 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 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 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 formation of alpha5 beta1-integrin FBs and for fibronectin fibrillogenesis, and (ii) the talin/tensin3 interaction drives this process, with vinculin acting to potentiate it.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: Suat Peng Neo

LAB HEAD: Jayantha Gunaratne

PROVIDER: PXD026343 | Pride | 2022-09-09

REPOSITORIES: Pride

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			Action	DRS
	TBP_QE_P4_200303_05_G822L3_G01.raw	Raw
	TBP_QE_P4_200303_06_G822L3_G02.raw	Raw
	TBP_QE_P4_200303_07_G822L3_G03.raw	Raw
	TBP_QE_P4_200303_08_G822L3_G04.raw	Raw
	TBP_QE_P4_200303_09_G822L3_G05.raw	Raw

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Tensin3 interaction with talin drives formation of fibronectin-associated fibrillar adhesions

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