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Embryos have a remarkable ability to repair wounds rapidly, with no inflammation or scarring. Embryonic wound healing is driven by the collective movement of the surrounding cells to seal the lesion. During embryonic wound closure, the cells adjacent to the wound polarize the cytoskeletal protein actin and the molecular motor non-muscle myosin II, which accumulate at the wound edge forming a supracellular cable around the wound. Adherens junction proteins including E-cadherin are internalized from the interface with the lesion and localize to former tricellular junctions at the wound margin, in a process necessary for cytoskeletal polarity. Using quantitative live microscopy, we found that the cells adjacent to wounds in theDrosophilaepidermis also polarized Talin, a core component of cell-extracellular matrix (ECM) adhesions that links integrins to the actin cytoskeleton. Integrin knock-down and inhibition of integrin binding delayed wound closure and were associated with a reduction in actin levels around the wound. Additionally, disrupting integrins caused a defect in E-cadherin reinforcement at tricellular junctions along the wound edge, suggesting crosstalk between integrin-based and cadherin-based adhesions. Together, our results show that cell-ECM adhesion contributes to embryonic wound repair and reveal an interplay between cell-cell and cell-ECM adhesion in the collective cell movements that drive rapid wound healing.