| Literature DB >> 11752628 |
H R de Jonge1, B Hogema, B C Tilly.
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.Entities:
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Year: 2000 PMID: 11752628 DOI: 10.1126/stke.2000.63.pe1
Source DB: PubMed Journal: Sci STKE ISSN: 1525-8882