Wound healing crucially relies on the mechanical activity of fibroblasts 
responding to TGFβ1 and to forces transmitted across focal adhesions. 
Integrin-linked kinase (ILK) is a central adapter recruited to integrin β1 tails 
in focal adhesions mediating the communication between cells and extracellular 
matrix. Here, we show that fibroblast-restricted inactivation of ILK in mice 
leads to impaired healing due to a severe reduction in the number of 
myofibroblasts, whereas inflammatory infiltrate and vascularization of the 
granulation tissue are unaffected. Primary ILK-deficient fibroblasts exhibit 
severely reduced levels of extracellular TGFβ1, α-smooth muscle actin (αSMA) 
production and myofibroblast conversion, which are rescued by exogenous TGFβ1. 
They are further characterized by elevated RhoA and low Rac1 activities, 
resulting in abnormal shape and reduced directional migration. Interference with 
RhoA-ROCK signaling largely restores morphology, migration and TGFβ1 levels. We 
conclude that, in fibroblasts, ILK is crucial for limiting RhoA activity, thus 
promoting TGFβ1 production, which is essential for dermal repair following 
injury.