Integrins are transmembrane receptors that mediate cell-cell or cell-matrix adhesion. All integrins are heterodimers composed of α and β subunits, which interact with extracellular matrix and cytoskeletal proteins. Signal transduction through intergin receptors may be regulated by integrin-linked kinase (ILK). ILK is a widely expressed Ser/Thr protein kinase that contains four ankyrin-like repeats in the N-terminal region, a phoshoinositide lipid-binding motif at amino acids 180-212, and an integrin binding site at amino acids 293-451. The ankyrin repeats interact with a LIM domain-only protein called PINCH that also binds the adaptor protein, Nck-2. This interaction implicates ILK in growth factor receptor pathways. The PINCH adaptor protein also contains a leucine-rich nuclear export signal and a nuclear localization signal. These two motifs implicate PINCH in nuclear functions, and in Schwann cells PINCH has been found in the nucleus, as well as, cytoplasm and perinuclear regions. Thus, PINCH is an adaptor protein that functions in both integrin signaling and nuclear functions.