| Literature DB >> 17873058 |
Rashna Bhandari1, 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.
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.Entities:
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Year: 2007 PMID: 17873058 PMCID: PMC2000531 DOI: 10.1073/pnas.0707338104
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205