The actin cytoskeleton is an essential network of filaments present in all cells and is important in many aspects of cell biology. It provides structure and support and is involved in cellular processes including adhesion, migration and proliferation. Members of the gelsolin family of actin-remodelling proteins regulate cytoskeletal organisation by severing and/or capping actin filaments. Manipulation of these proteins has revealed important roles for them in wound healing and scar formation. The absence of gelsolin leads to impaired healing with larger less contracted wounds related to its role in severing and remodelling actin filaments. In contrast, family member Flightless I (Flii) inhibits healing and decreasing its activity results in improved cellular adhesion, proliferation and migration. Wounds in mice with reduced levels of Flii heal significantly better than mice with normal levels and topical application of Flii neutralising antibodies improve healing in acute, diabetic and burn injuries models. Healing is accompanied by improved matrix deposition, reduced inflammation and a robust angiogenic response. Both gelsolin and Flii are present in human plasma with gelsolin acting as a scavenger of actin released into the circulation after tissue injury. Flii is also present in human plasma and wound fluid and has been shown to have important roles in regulating inflammation and angiogenesis. This presentation will discuss the importance of the actin cytoskeleton in wound healing and scar formation and will describe the development of new therapeutic antibodies targeted at cytoskeletal protein Flii aimed at improving the healing of patients suffering from burns or chronic non-healing wounds.