Kindlin-2 cooperates with talin to activate integrins and induces cell spreading by directly binding paxillin

• DOI: 10.7554/elife.10130
• Publication Date: 2016-01-27T11:01:58Z
• Authors: Marina Theodosiou; Moritz Widmaier; Ralph T Böttcher; Emanuel Rognoni; Maik Veelders; Mitasha Bharadwaj; Armin Lambacher; Katharina Austen; Daniel J Müller; Roy Zent; Reinhard Fässler
• Keywords: Paxillin; Lamellipodium; FERM domain

Integrins require an activation step prior to ligand binding and signaling. How talin kindlin contribute these events in non-hematopoietic cells is poorly understood. Here we report that fibroblasts lacking either or failed activate β1 integrins, adhere fibronectin (FN) maintain their integrins a high affinity conformation induced by Mn(2+). Despite compromised integrin adhesion, Mn(2+) enabled talin- but not kindlin-deficient initiate spreading on FN. This isotropic was the ability of directly bind paxillin, which turn bound focal adhesion kinase (FAK) resulting FAK formation lamellipodia. Our findings show cooperatively leading FN subsequently assembles essential signaling node at newly formed sites talin-independent manner.