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Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event

Year: 2007
Type: article
Abstract: In a previous study, we showed that the inositol pyrophosphate diphosphoinositol pentakisphosphate (IP(7)) physiologically phosphorylates mammalian and yeast proteins. We now report that this phosphate transfer reflects pyrophosphorylation. Thus, proteins must be prephosphorylated by ATP to prime them for IP(7) phosphorylation. IP(7) phosphorylates synthetic phosphopeptides but not if their phosphates have been masked by methylation or pyrophosphorylation. Moreover, IP(7) phosphorylated peptides are more acid-labile and more resistant to phosphatases than ATP phosphorylated peptides, indicating a different type of phosphate bond. Pyrophosphorylation may represent a novel mode of signaling to proteins.
DOI: 10.1073/pnas.0707338104
Authors: Rashna Bhandari, Adolfo Saiardi, Yousef Ahmadibeni, Adele M. Snowman, Adam C. Resnick, Troels Z. Kristiansen, Henrik Molina, Akhilesh Pandey, J. Kent Werner, Krishna R. Juluri, Yong Xu, Glenn D. Prestwich, Keykavous Parang, Solomon H. Snyder
Institutions: Johns Hopkins University, Johns Hopkins Medicine, MRC Laboratory for Molecular Cell Biology, University College London, Medical Research Council, University of Rhode Island, University of Pennsylvania, University of Utah
Language: English
Open Access status: green
Funders: National Institutes of Health, U.S. Public Health Service, Medical Research Council, National Institute of Mental Health, National Institute on Drug Abuse, National Cancer Institute, National Institute of Neurological Disorders and Stroke
Awards: G1615557336, Molecular Dissection of Growth Factor Receptor Signaling, Neurochemical Actions of Psychotropic Drugs, G5437238147, G7243145451, Neurotransmitter Receptors, Phosphoinositide and Inositol Polyphosphate Probes, Neurochemical Actions of Psychotropic Drugs, G9000163564, G913113481
OpenAlex ID: W2094942425
FWCI: 4.135
Cites: 28
Cited by: 212
Related to: 10