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Science 17 December 2004:
Vol. 306. no. 5704, pp. 2053 - 2055
DOI: 10.1126/science.1107225
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Perspectives

SIGNAL TRANSDUCTION:
Unexpected Mediators of Protein Phosphorylation

John D. York and Tony Hunter

The classic way of regulating proteins is by adding phosphate groups to them (phosphorylation), a job normally carried out by enzymes called kinases. In their Perspective, York and Hunter discuss exciting work (Saiardi et al.) suggesting that kinases are in for some stiff competition. High-energy signaling molecules called inositol pyrophosphates are able to donate phosphate groups to proteins in a nonenzymatic fashion. This represents a new way for signals to be transduced in cells.

J. D. York is in the Department of Pharmacology and Cancer Biology, Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA. T. Hunter is at the Molecular and Cellular Biology Laboratory, Salk Research Institute, La Jolla, CA 92037, USA. E-mail: yorkj{at}duke.edu

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Cloning and Characterization of Two Human VIP1-like Inositol Hexakisphosphate and Diphosphoinositol Pentakisphosphate Kinases.
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Inhibition of chronic ulcerative colitis associated adenocarcinoma development in mice by inositol compounds.
J. Liao, D. N. Seril, A. L. Yang, G. G. Lu, and G.-Y. Yang (2007)
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An essential role for an inositol polyphosphate multikinase, Ipk2, in mouse embryogenesis and second messenger production.
J. P. Frederick, D. Mattiske, J. A. Wofford, L. C. Megosh, L. Y. Drake, S.-T. Chiou, B. L. M. Hogan, and J. D. York (2005)
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