Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event

Authors

Rasha Bhandari
Adolfo Saiardi
Yousef Ahmadibeni, University of Rhode Island
Adele M. Snowman
Adam C. Resnick
Troels Z. Kristiansen
Henrik Molina
Akhilesh Pandey
J. Kent Werner Jr.
Krishna R. Juluri
Yong Xu
Glenn D. Prestwich
Keykavous Parang, University of Rhode IslandFollow
Solomon H. Snyder, University of Rhode Island

Document Type

Article

Date of Original Version

2007

Department

Biomedical and Pharmaceutical Sciences

Abstract

In a previous study, we showed that the inositol pyrophosphate diphosphoinositol pentakisphosphate (IP₇) 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 IP₇ phosphorylation. IP₇ phosphorylates synthetic phosphopeptides but not if their phosphates have been masked by methylation or pyrophosphorylation. Moreover, IP₇ 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.

Citation/Publisher Attribution

Bhandari, R., Saiardi, A., Ahmadibeni, Y., Snowman, A. M., Resnick, A. C., Kristiansen, T. Z., Molina, H.,...Snyder, S. H. (2007). Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event. Proceedings of the National Academy of Sciences, 104(39), 15305-15310. doi: 10.1073/pnas.0707338104

Available at: https://doi.org/10.1073/pnas.0707338104