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Trends Biochem Sci. 1995 Jul;20(7):272-6.

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

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Department of Physiology and Biophysics, HSC, SUNY, Stony Brook, NY 11794-8661, USA.


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.

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