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Science 17 December 2004:
Vol. 306. no. 5704, pp. 2101 - 2105
DOI: 10.1126/science.1103344
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Reports

Phosphorylation of Proteins by Inositol Pyrophosphates

Adolfo Saiardi,1*{dagger} Rashna Bhandari,1* Adam C. Resnick,1 Adele M. Snowman,1 Solomon H. Snyder1,2,3{ddagger}

The inositol pyrophosphates IP7 and IP8 contain highly energetic pyrophosphate bonds. Although implicated in various biologic functions, their molecular sites of action have not been clarified. Using radiolabeled IP7, we detected phosphorylation of multiple eukaryotic proteins. We also observed phosphorylation of endogenous proteins by endogenous IP7 in yeast. Phosphorylation by IP7 is nonenzymatic and may represent a novel intracellular signaling mechanism.

1 Department of Neuroscience, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
2 Department of Pharmacology and Molecular Sciences, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
3 Department of Psychiatry and Behavioral Sciences, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.


* These authors contributed equally to this work.

{dagger} Present address: Medical Research Council (MRC) Laboratory for Molecular Cell Biology and Cell Biology Unit, University College London, Gower Street, London WC1E 6BT, UK.

{ddagger} To whom correspondence should be addressed. E-mail: ssnyder{at}bs.jhmi.edu

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