Human Paxillin (Pax) Protein

Background

Paxillin (PXN) is a focal adhesion-associated adaptor protein that regulates cell adhesion, migration, and cytoskeletal organization by interacting with integrins, growth factor receptors, and signaling proteins at focal adhesions. It contains LIM domains and LD motifs, enabling it to recruit structural and signaling molecules such as focal adhesion kinase (FAK), vinculin, and Src kinases, coordinating actin cytoskeletal dynamics and mechanotransduction. Paxillin is critical for integrin-mediated signaling pathways, linking extracellular matrix (ECM) cues to intracellular processes like cell movement, proliferation, and survival. It plays a key role in embryonic development, tissue remodeling, and wound healing by modulating focal adhesion turnover and actomyosin contractility. Dysregulation of paxillin promotes cancer progression, metastasis, and drug resistance by enhancing cell migration, invasion, and survival signaling. Knockout studies reveal defects in focal adhesion formation, impaired cell motility, and developmental abnormalities, highlighting its essential role in cell adhesion, cytoskeletal regulation, and mechanotransduction.