Abstract
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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphate / metabolism
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Amino Acid Sequence
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Amino Acid Substitution
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Animals
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Drosophila Proteins / metabolism
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Drosophila melanogaster
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Escherichia coli Proteins / metabolism
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Humans
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Inositol Phosphates / metabolism*
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Kinetics
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Magnesium / metabolism
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Mice
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Molecular Sequence Data
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Mutation
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Nuclear Proteins / chemistry
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Nuclear Proteins / metabolism*
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Phosphates / metabolism
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Phosphorylation
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Phosphotransferases (Phosphate Group Acceptor) / metabolism
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Protein Kinases / genetics
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Protein Kinases / metabolism
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Proteins / metabolism*
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RNA-Binding Proteins / chemistry
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RNA-Binding Proteins / metabolism*
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / metabolism*
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Serine / metabolism
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Signal Transduction
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Temperature
Substances
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Drosophila Proteins
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Escherichia coli Proteins
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Inositol Phosphates
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NSR1 protein, S cerevisiae
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Nuclear Proteins
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Phosphates
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Proteins
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RNA-Binding Proteins
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Saccharomyces cerevisiae Proteins
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1-diphosphoinositol pentakisphosphate
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Serine
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Adenosine Triphosphate
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Protein Kinases
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Phosphotransferases (Phosphate Group Acceptor)
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Magnesium