The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions.
Hydrophobic insertion of the acyl chain into the bilayer is necessary but not sufficient for the membrane binding of a myristoylated protein. The myristoylated alanine-rich C kinase substrate (MARCKS), Src, ADP-ribosylation factor and human immunodeficiency virus-1 matrix proteins also contain a cluster of basic residues that bind to acidic phospholipids; the hydrophobic and electrostatic interactions act together to anchor the protein to a membrane. For MARCKS, and perhaps other proteins, phosphorylation of serines within its basic cluster reduces the electrostatic attraction, producing translocation of the protein from the membrane to the cytosol by a simple 'electrostatic switch' mechanism.
McLaughlin
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Department of Physiology and Biophysics, HSC, SUNY, Stony Brook, NY 11794-8661, USA.
Aderem
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D002462:Cell Membrane / Q000378:metabolism*; D003196:Computer Graphics; D047908:Intracellular Signaling Peptides and Proteins; D008051:Lipid Bilayers / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008958:Models, Molecular; D019814:Myristic Acid; D009227:Myristic Acids / Q000378:metabolism*; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D011493:Protein Kinase C / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*
D047908:Intracellular Signaling Peptides and Proteins; D008051:Lipid Bilayers; C000619710:MARCKS protein, human; D008565:Membrane Proteins; D009227:Myristic Acids; D011506:Proteins; D019814:Myristic Acid; D000076250:Myristoylated Alanine-Rich C Kinase Substrate; D011493:Protein Kinase C