Fibrosis and tissue scarring are caused by persistent myofibroblasts that have failed to undergo apoptosis. Although myofibroblasts promote wound healing, their persistence can result in fibrotic scarring owing to the high levels of αv integrins they express; this leads to overproduction of extracellular matrix and activation of transforming growth factor beta (TGFβ) signaling. However, the pathways leading to αv integrin accumulation are not fully understood. In this study (p. 3481), Audrey Bernstein and co-workers focus on the deubiquitylase (DUB) USP10 because their earlier work suggested that αvβ5 integrin in myofibroblasts retain less ubiquitin, which could prevent their degradation. Using an ex vivo corneal organ model and primary corneal myofibroblasts, they show here that USP10 expression is induced after wounding. In agreement with this, silencing of USP10 in corneal myofibroblasts results in increased ubiquitylation of the β1 and β5 subunits of αv integrins. Conversely, USP10 overexpression leads to an increase in the levels of αvβ1 and αvβ5 integrins, accompanied by activation of TGFβ signaling and upregulation of fibrotic markers. Importantly, silencing of USP10 in the ex vivo corneal organ model decreases fibrosis and promotes wound healing. This work thus presents a new role for a DUB in controlling the fibrotic response by directly regulating the surface expression of integrins and raises the possibility that targeting USP10 could promote regenerative pathways.
USP10: a novel antifibrotic target
USP10: a novel antifibrotic target. J Cell Sci 15 October 2017; 130 (20): e2002. doi:
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