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Publication Detail
Phosphorylation of proteins by inositol pyrophosphates.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Saiardi A, Bhandari R, Resnick AC, Snowman AM, Snyder SH
  • Publication date:
  • Pagination:
    2101, 2105
  • Journal:
  • Volume:
  • Issue:
  • Status:
  • Country:
    United States
  • PII:
  • Language:
  • Keywords:
    Adenosine Triphosphate, Amino Acid Sequence, Amino Acid Substitution, Animals, Drosophila Proteins, Drosophila melanogaster, Escherichia coli Proteins, Humans, Inositol Phosphates, Kinetics, Magnesium, Mice, Molecular Sequence Data, Mutation, Nuclear Proteins, Phosphates, Phosphorylation, Phosphotransferases (Phosphate Group Acceptor), Protein Kinases, Proteins, RNA-Binding Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Serine, Signal Transduction, Temperature
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.
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