Global analysis of protein arginine methylation

Fangrong Zhang; Jakob Kerbl-Knapp; Maria J Rodriguez Colman; Andreas Meinitzer; Therese Macher; Nemanja Vujić; Sandra Fasching; Evelyne Jany-Luig; Melanie Korbelius; Katharina B Kuentzel; Maximilian Mack; Alena Akhmetshina; Anita Pirchheim; Margret Paar; Beate Rinner; Gerd Hörl; Ernst Steyrer; Ulrich Stelzl; Boudewijn Burgering; Tobias Eisenberg; Brigitte Pertschy; Dagmar Kratky; Tobias Madl

doi:10.1016/j.crmeth.2021.100016

Global analysis of protein arginine methylation

Fangrong Zhang, Jakob Kerbl-Knapp, Maria J Rodriguez Colman, Andreas Meinitzer, Therese Macher, Nemanja Vujić, Sandra Fasching, Evelyne Jany-Luig, Melanie Korbelius, Katharina B Kuentzel, Maximilian Mack, Alena Akhmetshina, Anita Pirchheim, Margret Paar, Beate Rinner, Gerd Hörl, Ernst Steyrer, Ulrich Stelzl, Boudewijn Burgering, Tobias EisenbergBrigitte Pertschy, Dagmar Kratky, Tobias Madl

Medical University of Graz

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

Abstract

Quantitative information about the levels and dynamics of post-translational modifications (PTMs) is critical for an understanding of cellular functions. Protein arginine methylation (ArgMet) is an important subclass of PTMs and is involved in a plethora of (patho)physiological processes. However, because of the lack of methods for global analysis of ArgMet, the link between ArgMet levels, dynamics, and (patho)physiology remains largely unknown. We utilized the high sensitivity and robustness of nuclear magnetic resonance (NMR) spectroscopy to develop a general method for the quantification of global protein ArgMet. Our NMR-based approach enables the detection of protein ArgMet in purified proteins, cells, organoids, and mouse tissues. We demonstrate that the process of ArgMet is a highly prevalent PTM and can be modulated by small-molecule inhibitors and metabolites and changes in cancer and during aging. Thus, our approach enables us to address a wide range of biological questions related to ArgMet in health and disease.

Original language	English
Article number	100016
Pages (from-to)	1-15
Journal	Cell reports methods
Volume	1
Issue number	2
DOIs	https://doi.org/10.1016/j.crmeth.2021.100016
Publication status	Published - 2021 Jun 21
Externally published	Yes

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Zhang, F., Kerbl-Knapp, J., Rodriguez Colman, M. J., Meinitzer, A., Macher, T., Vujić, N., Fasching, S., Jany-Luig, E., Korbelius, M., Kuentzel, K. B., Mack, M., Akhmetshina, A., Pirchheim, A., Paar, M., Rinner, B., Hörl, G., Steyrer, E., Stelzl, U., Burgering, B., ... Madl, T. (2021). Global analysis of protein arginine methylation. Cell reports methods, 1(2), 1-15. Article 100016. https://doi.org/10.1016/j.crmeth.2021.100016

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title = "Global analysis of protein arginine methylation",

abstract = "Quantitative information about the levels and dynamics of post-translational modifications (PTMs) is critical for an understanding of cellular functions. Protein arginine methylation (ArgMet) is an important subclass of PTMs and is involved in a plethora of (patho)physiological processes. However, because of the lack of methods for global analysis of ArgMet, the link between ArgMet levels, dynamics, and (patho)physiology remains largely unknown. We utilized the high sensitivity and robustness of nuclear magnetic resonance (NMR) spectroscopy to develop a general method for the quantification of global protein ArgMet. Our NMR-based approach enables the detection of protein ArgMet in purified proteins, cells, organoids, and mouse tissues. We demonstrate that the process of ArgMet is a highly prevalent PTM and can be modulated by small-molecule inhibitors and metabolites and changes in cancer and during aging. Thus, our approach enables us to address a wide range of biological questions related to ArgMet in health and disease.",

author = "Fangrong Zhang and Jakob Kerbl-Knapp and {Rodriguez Colman}, {Maria J} and Andreas Meinitzer and Therese Macher and Nemanja Vuji{\'c} and Sandra Fasching and Evelyne Jany-Luig and Melanie Korbelius and Kuentzel, {Katharina B} and Maximilian Mack and Alena Akhmetshina and Anita Pirchheim and Margret Paar and Beate Rinner and Gerd H{\"o}rl and Ernst Steyrer and Ulrich Stelzl and Boudewijn Burgering and Tobias Eisenberg and Brigitte Pertschy and Dagmar Kratky and Tobias Madl",

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doi = "10.1016/j.crmeth.2021.100016",

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Zhang, F, Kerbl-Knapp, J, Rodriguez Colman, MJ, Meinitzer, A, Macher, T, Vujić, N, Fasching, S, Jany-Luig, E, Korbelius, M, Kuentzel, KB, Mack, M, Akhmetshina, A, Pirchheim, A, Paar, M, Rinner, B, Hörl, G, Steyrer, E, Stelzl, U, Burgering, B, Eisenberg, T, Pertschy, B, Kratky, D & Madl, T 2021, 'Global analysis of protein arginine methylation', Cell reports methods, vol. 1, no. 2, 100016, pp. 1-15. https://doi.org/10.1016/j.crmeth.2021.100016

TY - JOUR

T1 - Global analysis of protein arginine methylation

AU - Zhang, Fangrong

AU - Kerbl-Knapp, Jakob

AU - Rodriguez Colman, Maria J

AU - Meinitzer, Andreas

AU - Macher, Therese

AU - Vujić, Nemanja

AU - Fasching, Sandra

AU - Jany-Luig, Evelyne

AU - Korbelius, Melanie

AU - Kuentzel, Katharina B

AU - Mack, Maximilian

AU - Akhmetshina, Alena

AU - Pirchheim, Anita

AU - Paar, Margret

AU - Rinner, Beate

AU - Hörl, Gerd

AU - Steyrer, Ernst

AU - Stelzl, Ulrich

AU - Burgering, Boudewijn

AU - Eisenberg, Tobias

AU - Pertschy, Brigitte

AU - Kratky, Dagmar

AU - Madl, Tobias

PY - 2021/6/21

Y1 - 2021/6/21

N2 - Quantitative information about the levels and dynamics of post-translational modifications (PTMs) is critical for an understanding of cellular functions. Protein arginine methylation (ArgMet) is an important subclass of PTMs and is involved in a plethora of (patho)physiological processes. However, because of the lack of methods for global analysis of ArgMet, the link between ArgMet levels, dynamics, and (patho)physiology remains largely unknown. We utilized the high sensitivity and robustness of nuclear magnetic resonance (NMR) spectroscopy to develop a general method for the quantification of global protein ArgMet. Our NMR-based approach enables the detection of protein ArgMet in purified proteins, cells, organoids, and mouse tissues. We demonstrate that the process of ArgMet is a highly prevalent PTM and can be modulated by small-molecule inhibitors and metabolites and changes in cancer and during aging. Thus, our approach enables us to address a wide range of biological questions related to ArgMet in health and disease.

AB - Quantitative information about the levels and dynamics of post-translational modifications (PTMs) is critical for an understanding of cellular functions. Protein arginine methylation (ArgMet) is an important subclass of PTMs and is involved in a plethora of (patho)physiological processes. However, because of the lack of methods for global analysis of ArgMet, the link between ArgMet levels, dynamics, and (patho)physiology remains largely unknown. We utilized the high sensitivity and robustness of nuclear magnetic resonance (NMR) spectroscopy to develop a general method for the quantification of global protein ArgMet. Our NMR-based approach enables the detection of protein ArgMet in purified proteins, cells, organoids, and mouse tissues. We demonstrate that the process of ArgMet is a highly prevalent PTM and can be modulated by small-molecule inhibitors and metabolites and changes in cancer and during aging. Thus, our approach enables us to address a wide range of biological questions related to ArgMet in health and disease.

U2 - 10.1016/j.crmeth.2021.100016

DO - 10.1016/j.crmeth.2021.100016

M3 - Article

C2 - 35475236

SN - 2667-2375

VL - 1

SP - 1

EP - 15

JO - Cell reports methods

JF - Cell reports methods

IS - 2

M1 - 100016

ER -

Global analysis of protein arginine methylation

Abstract

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