Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event

Rashna Bhandari; Adolfo Saiardi; Yousef Ahmadibeni; Adele M. Snowman; Resnick C. Adam; Troels Z. Kristiansen; Henrik Molina; Akhilesh Pandey; J. Kent Werner; Krishna R. Juluri; Yong Ku; Glenn D. Prestwich; Keykavous Parang; Solomon H. Snyder

doi:10.1073/pnas.0707338104

Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event

Rashna Bhandari, Adolfo Saiardi, Yousef Ahmadibeni, Adele M. Snowman, Resnick C. Adam, Troels Z. Kristiansen, Henrik Molina, Akhilesh Pandey, J. Kent Werner, Krishna R. Juluri, Yong Ku, Glenn D. Prestwich, Keykavous Parang, Solomon H. Snyder^*

^*Corresponding author for this work

Neurology

Research output: Contribution to journal › Article › peer-review

187 Scopus citations

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 reprissent a novel mode of signaling to proteins.

Original language	English
Pages (from-to)	15305-15310
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	104
Issue number	39
DOIs	https://doi.org/10.1073/pnas.0707338104
State	Published - 25 Sep 2007

Keywords

Inositol polyphosphate
Protein phosphorylation

Access to Document

10.1073/pnas.0707338104

Cite this

Bhandari, R., Saiardi, A., Ahmadibeni, Y., Snowman, A. M., Adam, R. C., Kristiansen, T. Z., Molina, H., Pandey, A., Werner, J. K., Juluri, K. R., Ku, Y., Prestwich, G. D., Parang, K., & Snyder, S. H. (2007). Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event. Proceedings of the National Academy of Sciences of the United States of America, 104(39), 15305-15310. https://doi.org/10.1073/pnas.0707338104

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title = "Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event",

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 reprissent a novel mode of signaling to proteins.",

keywords = "Inositol polyphosphate, Protein phosphorylation",

author = "Rashna Bhandari and Adolfo Saiardi and Yousef Ahmadibeni and Snowman, {Adele M.} and Adam, {Resnick C.} and Kristiansen, {Troels Z.} and Henrik Molina and Akhilesh Pandey and Werner, {J. Kent} and Juluri, {Krishna R.} and Yong Ku and Prestwich, {Glenn D.} and Keykavous Parang and Snyder, {Solomon H.}",

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Bhandari, R, Saiardi, A, Ahmadibeni, Y, Snowman, AM, Adam, RC, Kristiansen, TZ, Molina, H, Pandey, A, Werner, JK, Juluri, KR, Ku, Y, Prestwich, GD, Parang, K & Snyder, SH 2007, 'Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event', Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 39, pp. 15305-15310. https://doi.org/10.1073/pnas.0707338104

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T1 - Protein pyrophosphorylation by inositol pyrophosphates is a posttranslational event

AU - Bhandari, Rashna

AU - Saiardi, Adolfo

AU - Ahmadibeni, Yousef

AU - Snowman, Adele M.

AU - Adam, Resnick C.

AU - Kristiansen, Troels Z.

AU - Molina, Henrik

AU - Pandey, Akhilesh

AU - Werner, J. Kent

AU - Juluri, Krishna R.

AU - Ku, Yong

AU - Prestwich, Glenn D.

AU - Parang, Keykavous

AU - Snyder, Solomon H.

PY - 2007/9/25

Y1 - 2007/9/25

N2 - 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 reprissent a novel mode of signaling to proteins.

AB - 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 reprissent a novel mode of signaling to proteins.

KW - Inositol polyphosphate

KW - Protein phosphorylation

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