Global analysis of protein arginine methylation
(2021) In Cell reports methods 1(2). p.1-15- 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.... (More)
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.
(Less)
- author
- publishing date
- 2021-06-21
- type
- Contribution to journal
- publication status
- published
- in
- Cell reports methods
- volume
- 1
- issue
- 2
- article number
- 100016
- pages
- 1 - 15
- publisher
- Cell Press
- external identifiers
-
- scopus:85111768121
- pmid:35475236
- ISSN
- 2667-2375
- DOI
- 10.1016/j.crmeth.2021.100016
- language
- English
- LU publication?
- no
- additional info
- © 2021 The Authors.
- id
- 1da6a07e-5d46-4a28-b074-f1c1f20a8dc7
- date added to LUP
- 2022-10-10 16:30:02
- date last changed
- 2024-06-27 15:57:33
@article{1da6a07e-5d46-4a28-b074-f1c1f20a8dc7, abstract = {{<p>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.</p>}}, author = {{Zhang, Fangrong and Kerbl-Knapp, Jakob and Rodriguez Colman, Maria J and Meinitzer, Andreas and Macher, Therese and Vujić, Nemanja and Fasching, Sandra and Jany-Luig, Evelyne and Korbelius, Melanie and Kuentzel, Katharina B and Mack, Maximilian and Akhmetshina, Alena and Pirchheim, Anita and Paar, Margret and Rinner, Beate and Hörl, Gerd and Steyrer, Ernst and Stelzl, Ulrich and Burgering, Boudewijn and Eisenberg, Tobias and Pertschy, Brigitte and Kratky, Dagmar and Madl, Tobias}}, issn = {{2667-2375}}, language = {{eng}}, month = {{06}}, number = {{2}}, pages = {{1--15}}, publisher = {{Cell Press}}, series = {{Cell reports methods}}, title = {{Global analysis of protein arginine methylation}}, url = {{http://dx.doi.org/10.1016/j.crmeth.2021.100016}}, doi = {{10.1016/j.crmeth.2021.100016}}, volume = {{1}}, year = {{2021}}, }