Paxillin is a focal adhesion (FA) adapter protein that controls integrin-signaling. However, its binding mechanism to this complex is not understood. This study shows that compromising paxillin interactions with FAs causes rapid adhesion sliding, which could be rescued by inducing mechanical coupling of paxillin to integrins via bimolecular fluorescence complementation. While confirming the previously proposed FA-targeting function of the paxillin LIM domains, this work demonstrates specific contributions of each LIM domain to FA binding, which have been revealed by combining difference fluorescnce imaging approaches such as live cell imaging, photoactivation, FRAP, FA-isolation and bimolecular fluorescence complementation.