Protein N-myristoylation: Critical Role in Apoptosis and Salt Tolerance
Hugo R. de Jonge,
Boris Hogema, and
Ben C. Tilly
The authors are at the Department of Biochemistry, Cardiovascular Research Institute COEUR, Faculty of Medicine and Health Sciences, Erasmus University, Post Office Box 1738, 3000DR Rotterdam, The Netherlands. E-mail: dejonge{at}bc1.fgg.eur.nl
Abstract:
N-myristoylation is a covalent protein modification that can promote the association of proteins with membranes. De Jonge, Hogema, and Tilly discuss how N-myristoylation may be involved in triggering Fas ligand-induced apoptosis in mammals, and in adapting to conditions of high salt in plants. The pro-apoptotic protein BID is unique in that its proteolytic cleavage product, tBID, is posttranslationally myristoylated. In contrast, the plant accessory protein SOS3 undergoes "classical" cotranslational N-myristoylation. N-myristoylation is essential for the proper functioning of these proteins in regulating the signaling pathways (apoptosis and adaptation to salt stress, respectively) in which they are involved.
