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Molecular mechanics of calcium-myristoyl switches.

Ames JB, Ishima R, Tanaka T, Gordon JI, Stryer L, Ikura M
Nature 389 198-202 (1997)
Cited: 282 times
EuropePMC logo PMID: 9296500

Abstract

Many eukaryotic cellular and viral proteins have a covalently attached myristoyl group at the amino terminus. One such protein is recoverin, a calcium sensor in retinal rod cells, which controls the lifetime of photoexcited rhodopsin by inhibiting rhodopsin kinase. Recoverin has a relative molecular mass of 23,000 (M[r] 23K), and contains an amino-terminal myristoyl group (or related acyl group) and four EF hands. The binding of two Ca2+ ions to recoverin leads to its translocation from the cytosol to the disc membrane. In the Ca2+-free state, the myristoyl group is sequestered in a deep hydrophobic box, where it is clamped by multiple residues contributed by three of the EF hands. We have used nuclear magnetic resonance to show that Ca2+ induces the unclamping and extrusion of the myristoyl group, enabling it to interact with a lipid bilayer membrane. The transition is also accompanied by a 45-degree rotation of the amino-terminal domain relative to the carboxy-terminal domain, and many hydrophobic residues are exposed. The conservation of the myristoyl binding site and two swivels in recoverin homologues from yeast to humans indicates that calcium-myristoyl switches are ancient devices for controlling calcium-sensitive processes.

Reviews - 1jsa mentioned but not cited (3)

  1. Protein and Signaling Networks in Vertebrate Photoreceptor Cells. Koch KW, Dell'Orco D. Front Mol Neurosci 8 67 (2015)
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Articles - 1jsa mentioned but not cited (12)

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