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The Alarmone Diadenosine Tetraphosphate as a Cosubstrate for Protein AMPylation

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The Alarmone Diadenosine Tetraphosphate as a Cosubstrate for Protein AMPylation. / Frese, Matthias; Saumer, Philip; Yuan, Yizhi; Herzog, Doreen; Höpfner, Dorothea; Itzen, Aymelt; Marx, Andreas.

in: ANGEW CHEM INT EDIT, Jahrgang 62, Nr. 8, e202213279, 13.02.2023, S. e202213279.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Frese, M, Saumer, P, Yuan, Y, Herzog, D, Höpfner, D, Itzen, A & Marx, A 2023, 'The Alarmone Diadenosine Tetraphosphate as a Cosubstrate for Protein AMPylation', ANGEW CHEM INT EDIT, Jg. 62, Nr. 8, e202213279, S. e202213279. https://doi.org/10.1002/anie.202213279

APA

Frese, M., Saumer, P., Yuan, Y., Herzog, D., Höpfner, D., Itzen, A., & Marx, A. (2023). The Alarmone Diadenosine Tetraphosphate as a Cosubstrate for Protein AMPylation. ANGEW CHEM INT EDIT, 62(8), e202213279. [e202213279]. https://doi.org/10.1002/anie.202213279

Vancouver

Frese M, Saumer P, Yuan Y, Herzog D, Höpfner D, Itzen A et al. The Alarmone Diadenosine Tetraphosphate as a Cosubstrate for Protein AMPylation. ANGEW CHEM INT EDIT. 2023 Feb 13;62(8):e202213279. e202213279. https://doi.org/10.1002/anie.202213279

Bibtex

@article{713a8631d1cd4fea8594c8e7ca31a5db,
title = "The Alarmone Diadenosine Tetraphosphate as a Cosubstrate for Protein AMPylation",
abstract = "Diadenosine polyphosphates (Apn As) are non-canonical nucleotides whose cellular concentrations increase during stress and are therefore termed alarmones, signaling homeostatic imbalance. Their cellular role is poorly understood. In this work, we assessed Apn As for their usage as cosubstrates for protein AMPylation, a post-translational modification in which adenosine monophosphate (AMP) is transferred to proteins. In humans, AMPylation mediated by the AMPylator FICD with ATP as a cosubstrate is a response to ER stress. Herein, we demonstrate that Ap4 A is proficiently consumed for AMPylation by FICD. By chemical proteomics using a new chemical probe, we identified new potential AMPylation targets. Interestingly, we found that AMPylation targets of FICD may differ depending on the nucleotide cosubstrate. These results may suggest that signaling at elevated Ap4 A levels during cellular stress differs from when Ap4 A is present at low concentrations, allowing response to extracellular cues.",
author = "Matthias Frese and Philip Saumer and Yizhi Yuan and Doreen Herzog and Dorothea H{\"o}pfner and Aymelt Itzen and Andreas Marx",
note = "{\textcopyright} 2022 Wiley-VCH GmbH.",
year = "2023",
month = feb,
day = "13",
doi = "10.1002/anie.202213279",
language = "English",
volume = "62",
pages = "e202213279",
journal = "ANGEW CHEM INT EDIT",
issn = "1433-7851",
publisher = "John Wiley and Sons Ltd",
number = "8",

}

RIS

TY - JOUR

T1 - The Alarmone Diadenosine Tetraphosphate as a Cosubstrate for Protein AMPylation

AU - Frese, Matthias

AU - Saumer, Philip

AU - Yuan, Yizhi

AU - Herzog, Doreen

AU - Höpfner, Dorothea

AU - Itzen, Aymelt

AU - Marx, Andreas

N1 - © 2022 Wiley-VCH GmbH.

PY - 2023/2/13

Y1 - 2023/2/13

N2 - Diadenosine polyphosphates (Apn As) are non-canonical nucleotides whose cellular concentrations increase during stress and are therefore termed alarmones, signaling homeostatic imbalance. Their cellular role is poorly understood. In this work, we assessed Apn As for their usage as cosubstrates for protein AMPylation, a post-translational modification in which adenosine monophosphate (AMP) is transferred to proteins. In humans, AMPylation mediated by the AMPylator FICD with ATP as a cosubstrate is a response to ER stress. Herein, we demonstrate that Ap4 A is proficiently consumed for AMPylation by FICD. By chemical proteomics using a new chemical probe, we identified new potential AMPylation targets. Interestingly, we found that AMPylation targets of FICD may differ depending on the nucleotide cosubstrate. These results may suggest that signaling at elevated Ap4 A levels during cellular stress differs from when Ap4 A is present at low concentrations, allowing response to extracellular cues.

AB - Diadenosine polyphosphates (Apn As) are non-canonical nucleotides whose cellular concentrations increase during stress and are therefore termed alarmones, signaling homeostatic imbalance. Their cellular role is poorly understood. In this work, we assessed Apn As for their usage as cosubstrates for protein AMPylation, a post-translational modification in which adenosine monophosphate (AMP) is transferred to proteins. In humans, AMPylation mediated by the AMPylator FICD with ATP as a cosubstrate is a response to ER stress. Herein, we demonstrate that Ap4 A is proficiently consumed for AMPylation by FICD. By chemical proteomics using a new chemical probe, we identified new potential AMPylation targets. Interestingly, we found that AMPylation targets of FICD may differ depending on the nucleotide cosubstrate. These results may suggest that signaling at elevated Ap4 A levels during cellular stress differs from when Ap4 A is present at low concentrations, allowing response to extracellular cues.

U2 - 10.1002/anie.202213279

DO - 10.1002/anie.202213279

M3 - SCORING: Journal article

C2 - 36524454

VL - 62

SP - e202213279

JO - ANGEW CHEM INT EDIT

JF - ANGEW CHEM INT EDIT

SN - 1433-7851

IS - 8

M1 - e202213279

ER -