Protein Pyrophosphorylation by Inositol Pyrophosphates is a Posttranslational Event

Authors

Rashna Bhandari, Columbia University
Adolfo Saiardi, University College London
Yousef Ahmadibeni, University of Rhode IslandFollow
Adele M. Snowman, Johns Hopkins University
Adam C. Resnick, University of Pennsylvania
Troels Z. Kristiansen, Johns Hopkins University
Henrik Molina, Rambam Health Care Center
Akhilesh Pandey, University of Tennessee
J. Kent Werner Jr., Johns Hopkins University
Krishna R. Juluri, Johns Hopkins University
Yong Xu, SUNY Stony Brook
Glenn D. Prestwich, University of Utah
Keykavous Parang, Chapman UniversityFollow
Solomon H. Snyder, Johns Hopkins University

Document Type

Article

Publication Date

2007

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 ATIP 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 ATIP phosphorylated peptides, indicating a different type of phosphate bond. Pyrophosphorylation may represent a novel mode of signaling to proteins.

Comments

This article was originally published in Proceedings of the National Academy of Sciences, volume 104, issue 39, in 2007. DOI: 10.1073/pnas.0707338104

Recommended Citation

Bhandari, Rashna, Adolfo Saiardi, Yousef Ahmadibeni, Adele M. Snowman, Adam C. Resnick, Troels Z. Kristiansen, Henrik Molina et al. "Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event." Proceedings of the National Academy of Sciences 104, no. 39 (2007): 15305-15310.
DOI:10.1073/pnas.0707338104

Copyright

National Academy of Sciences