The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions

Trends Biochem Sci. 1995 Jul;20(7):272-6. doi: 10.1016/s0968-0004(00)89042-8.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Cell Membrane / metabolism*
  • Computer Graphics
  • Intracellular Signaling Peptides and Proteins*
  • Lipid Bilayers / metabolism
  • Membrane Proteins / metabolism
  • Models, Molecular
  • Myristic Acid
  • Myristic Acids / metabolism*
  • Myristoylated Alanine-Rich C Kinase Substrate
  • Protein Kinase C / metabolism
  • Proteins / metabolism*


  • Intracellular Signaling Peptides and Proteins
  • Lipid Bilayers
  • MARCKS protein, human
  • Membrane Proteins
  • Myristic Acids
  • Proteins
  • Myristic Acid
  • Myristoylated Alanine-Rich C Kinase Substrate
  • Protein Kinase C