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Phosphorylation of proteins by inositol pyrophosphates.
- Source :
-
Science (New York, N.Y.) [Science] 2004 Dec 17; Vol. 306 (5704), pp. 2101-5. - Publication Year :
- 2004
-
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.
- Subjects :
- Adenosine Triphosphate metabolism
Amino Acid Sequence
Amino Acid Substitution
Animals
Drosophila Proteins metabolism
Drosophila melanogaster
Escherichia coli Proteins metabolism
Humans
Kinetics
Magnesium metabolism
Mice
Molecular Sequence Data
Mutation
Nuclear Proteins chemistry
Phosphates metabolism
Phosphorylation
Phosphotransferases (Phosphate Group Acceptor) metabolism
Protein Kinases genetics
Protein Kinases metabolism
RNA-Binding Proteins chemistry
Saccharomyces cerevisiae metabolism
Saccharomyces cerevisiae Proteins chemistry
Serine metabolism
Signal Transduction
Temperature
Inositol Phosphates metabolism
Nuclear Proteins metabolism
Proteins metabolism
RNA-Binding Proteins metabolism
Saccharomyces cerevisiae Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1095-9203
- Volume :
- 306
- Issue :
- 5704
- Database :
- MEDLINE
- Journal :
- Science (New York, N.Y.)
- Publication Type :
- Academic Journal
- Accession number :
- 15604408
- Full Text :
- https://doi.org/10.1126/science.1103344