Fibronectins: Structural-functional relationships

Abstract

This review summarized current data on the structure of fibronectin (FN), a multifunctional glycoprotein of vertebrates. FN is not only a permanent component of the extracellular matrix (ECM) but also an important regulator of cell functions via transformation of the ECM composition and organization and/or interaction with receptor and other membranebound cell proteins. Multifunctionality of FN owes hierarchical relationships between its structuralfunctional determinants, which comprise the linear ones (FN peptide fragments), association zones (surface contacts between the FN molecule and a FN-associated protein) and functional domains (those binding fibrin, heparin, gelatin and integrins). The modular architectonic principle of FN organization is pivotal to intrinsic adaptation of this glycoprotein to changing microenvironmental conditions. We also discuss the issue of key stages of FN fibrillogenesis with a special focus on the molecular mechanisms that underlie polymerization of FN molecules.