Morphology of senescent cells is constantly changing at the molecular level, which in turn leads to disruption of their function. It is connected with reduced ability to synthesize extracellular matrix (ECM) and leads to the dysfunction of integrin adhesion molecules and adhesion clusters. In skin, these factors cause a loss of communication between the extracellular matrix and fibroblasts. This contributes to the appearance of signs of aging. The aim of this study is to draw attention to the very important molecule such as paxillin, which is an adaptor protein with mass of 68 kDa. This family of proteins includes Hic-5, PaxB and leupaxin. Paxillin binds to actin-binding proteins such as vinculin, actopaxin, and kinases (e.g. Integrin-linked kinase (ILK)). Moreover, it plays an important role in the integrity of the matrix, because it transduces transmembrane signaling between integrins and growth factors. Paxillin is a scaffold protein, activating the arrangement and organization of the cytoskeleton. Signaling through paxillin affects the long-term changes in gene expression, cell proliferation, and organization of the ECM. Correct functioning of the ECM is important for the wound healing processes and regeneration of tissues or tissue repair. Decrease or lack of paxillin expression results in changes in the structure and integrity of the ECM, which are manifested by aging of cells and organs. Restoration of the cellular matrix connections would be a significant element in the processes related to the anti-aging activities.