Pathways crossing mammalian and plant sulfenomic landscapes
- Author
- Jingjing Huang (UGent) , Patrick Willems (UGent) , Frank Van Breusegem (UGent) and Joris Messens
- Organization
- Abstract
- Reactive oxygen species (ROS) and especially hydrogen peroxide, are potent signaling molecules that activate cellular defense responses. Hydrogen peroxide can provoke reversible and irreversible oxidative posttranslational modifications on cysteine residues of proteins that act in diverse signaling circuits. The initial oxidation product of cysteine, sulfenic acid, has emerged as a biologically relevant posttranslational modification, because it is the primary sulfur oxygen modification that precedes divergent series of additional adaptations. In this review, we focus on the functional consequences of sulfenylation for both mammalian and plant proteins. Furthermore, we created compendia of sulfenylated proteins in human and plants based on mass spectrometry experiments, thereby defining the current plant and human sulfenomes. To assess the evolutionary conservation of sulfenylation, the sulfenomes of human and plants were compared based on protein homology. In total, 185 human sulfenylated proteins showed homology to sulfenylated plant proteins and the conserved sulfenylation targets participated in specific biological pathways and metabolic processes. Comprehensive functional studies of sulfenylation remains a future challenge, with multiple candidates suggested by mass spectrometry awaiting scrutinization.
- Keywords
- CYSTEINE-SULFINIC ACID, NF-KAPPA-B, GENETICALLY ENCODED PROBE, END RULE, PATHWAY, ARABIDOPSIS-THALIANA, HYDROGEN-PEROXIDE, REDOX REGULATION, S-NITROSYLATION, GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, OXIDATIVE, STRESS, Redox signaling, Cysteine oxidation, Sulfenic acid
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-8577874
- MLA
- Huang, Jingjing, et al. “Pathways Crossing Mammalian and Plant Sulfenomic Landscapes.” FREE RADICAL BIOLOGY AND MEDICINE, vol. 122, 2018, pp. 193–201, doi:10.1016/j.freeradbiomed.2018.02.012.
- APA
- Huang, J., Willems, P., Van Breusegem, F., & Messens, J. (2018). Pathways crossing mammalian and plant sulfenomic landscapes. FREE RADICAL BIOLOGY AND MEDICINE, 122, 193–201. https://doi.org/10.1016/j.freeradbiomed.2018.02.012
- Chicago author-date
- Huang, Jingjing, Patrick Willems, Frank Van Breusegem, and Joris Messens. 2018. “Pathways Crossing Mammalian and Plant Sulfenomic Landscapes.” FREE RADICAL BIOLOGY AND MEDICINE 122: 193–201. https://doi.org/10.1016/j.freeradbiomed.2018.02.012.
- Chicago author-date (all authors)
- Huang, Jingjing, Patrick Willems, Frank Van Breusegem, and Joris Messens. 2018. “Pathways Crossing Mammalian and Plant Sulfenomic Landscapes.” FREE RADICAL BIOLOGY AND MEDICINE 122: 193–201. doi:10.1016/j.freeradbiomed.2018.02.012.
- Vancouver
- 1.Huang J, Willems P, Van Breusegem F, Messens J. Pathways crossing mammalian and plant sulfenomic landscapes. FREE RADICAL BIOLOGY AND MEDICINE. 2018;122:193–201.
- IEEE
- [1]J. Huang, P. Willems, F. Van Breusegem, and J. Messens, “Pathways crossing mammalian and plant sulfenomic landscapes,” FREE RADICAL BIOLOGY AND MEDICINE, vol. 122, pp. 193–201, 2018.
@article{8577874,
abstract = {{Reactive oxygen species (ROS) and especially hydrogen peroxide, are potent signaling molecules that activate cellular defense responses. Hydrogen peroxide can provoke reversible and irreversible oxidative posttranslational modifications on cysteine residues of proteins that act in diverse signaling circuits. The initial oxidation product of cysteine, sulfenic acid, has emerged as a biologically relevant posttranslational modification, because it is the primary sulfur oxygen modification that precedes divergent series of additional adaptations. In this review, we focus on the functional consequences of sulfenylation for both mammalian and plant proteins. Furthermore, we created compendia of sulfenylated proteins in human and plants based on mass spectrometry experiments, thereby defining the current plant and human sulfenomes. To assess the evolutionary conservation of sulfenylation, the sulfenomes of human and plants were compared based on protein homology. In total, 185 human sulfenylated proteins showed homology to sulfenylated plant proteins and the conserved sulfenylation targets participated in specific biological pathways and metabolic processes. Comprehensive functional studies of sulfenylation remains a future challenge, with multiple candidates suggested by mass spectrometry awaiting scrutinization.}},
author = {{Huang, Jingjing and Willems, Patrick and Van Breusegem, Frank and Messens, Joris}},
issn = {{0891-5849}},
journal = {{FREE RADICAL BIOLOGY AND MEDICINE}},
keywords = {{CYSTEINE-SULFINIC ACID,NF-KAPPA-B,GENETICALLY ENCODED PROBE,END RULE,PATHWAY,ARABIDOPSIS-THALIANA,HYDROGEN-PEROXIDE,REDOX REGULATION,S-NITROSYLATION,GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE,OXIDATIVE,STRESS,Redox signaling,Cysteine oxidation,Sulfenic acid}},
language = {{eng}},
pages = {{193--201}},
title = {{Pathways crossing mammalian and plant sulfenomic landscapes}},
url = {{http://doi.org/10.1016/j.freeradbiomed.2018.02.012}},
volume = {{122}},
year = {{2018}},
}
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