Figure 1.

Schematic illustration of the integrin-linked kinase-protein kinase B (ILK-PKB) signaling pathway. Integrin-linked kinase forms, together with PINCH (particularly interesting Cys-His-rich protein) and parvin, the ILK-PINCH-parvin (IPP) complex and mediates signals from the extracellular matrix (ECM) to the cytoplasm through integrins. The phosphorylated downstream target PKB facilitates the expression of stretch responsive genes such as the atrial natriuretic factor (anf), thereby effectively transducing signals from the cardiac stretch sensor. Reduced PKB phosphorylation in ILK deficient main squeeze mutant zebrafish hearts was demonstrated to lead to impaired cardiac contractility and heart failure [10]. In this context, the inhibition of protein phosphatases (PP) by small chemical compounds that results in an increase of PKB phosphorylation might be a promising therapeutic approach to treat ILK-associated cardiomyopathies.