title: Protein myristoylation in protein-lipid and protein-protein interactions.
abstract: Various proteins in signal transduction pathways are myristoylated. Although this modification is often essential for the proper functioning of the modified protein, the mechanism by which the modification exerts its effects is still largely unknown. Here we discuss the roles played by protein myristoylation, in both protein-lipid and protein-protein interactions. Myristoylation is involved in the membrane interactions of various proteins, such as MARCKS and endothelial NO synthase. The intermediate hydrophobic nature of the modification plays an important role in the reversible membrane anchoring of these proteins. The anchoring is strengthened by a basic amphiphilic domain that works as a switch for the reversible binding. Protein myristoylation is also involved in protein-protein interactions, which are regulated by the interplay between protein phosphorylation, calmodulin binding, and membrane phospholipids.
authors.affiliation: Institute of Comprehensive Medical Science, Fujita Health University, Toyoake, Japan. htanigut@fujita-hu.ac.jp
authors.forename: H
authors.initials: H
authors.lastname: Taniguchi
mesh_terms: D000595:Amino Acid Sequence; D047908:Intracellular Signaling Peptides and Proteins; D050356:Lipid Metabolism; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D019814:Myristic Acid / Q000378:metabolism*; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D011506:Proteins; D019814:Myristic Acid; D000076250:Myristoylated Alanine-Rich C Kinase Substrate