The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
Global Proteome Analyses of Lysine Acetylation and Succinylation Reveal the Widespread Involvement of both Modification in Metabolism in the Embryo of Germinating Rice Seed
Abstract
Regulation of rice seed germination has been shown to mainly occur at post-transcriptional levels, of which the changes on proteome status is a major one. Lysine acetylation and succinylation are two prevalent protein post-translational modifications (PTMs) involved in multiple biological processes, especially for metabolism regulation. To investigate the potential mechanism controlling metabolism regulation in rice seed germination, we performed the lysine acetylation and succinylation analyses simultaneously. Using high-accuracy nano-LC-MS/MS in combination with the enrichment of lysine acetylated or succinylated peptides from digested embryonic proteins of 24 h after imbibition (HAI) rice seed, a total of 699 acetylated sites from 389 proteins and 665 succinylated sites from 261 proteins were identified. Among these modified lysine sites, 133 sites on 78 proteins were commonly modified by two PTMs. The overlapped PTM sites were more likely to be in polar acidic/basic amino acid regions and exposed on the protein surface. Both of the acetylated and succinylated proteins cover nearly all aspects of cellular functions. Ribosome complex and glycolysis/gluconeogenesis-related proteins were significantly enriched in both acetylated and succinylated protein profiles through KEGG enrichment and protein-protein interaction network analyses. The acetyl-CoA and succinyl-CoA metabolism-related enzymes were found to be extensively modified by both modifications, implying the functional interaction between the two PTMs. This study provides a rich resource to examine the modulation of the two PTMs on the metabolism pathway and other biological processes in germinating rice seed.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“However, it must also be noted that, compared with malonate, itaconate is a relatively weak competitive inhibitor of SDH47,49, which raised the question as to whether any additional mechanisms could contribute to the anti-inflammatory effects of itaconate.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [49]
In the citing paper
“By employing a proteomic approach the authors discovered a range of proteins which regulate T cell function that are sensitive to covalent modification by DMF including protein kinase C θ (PKCθ).”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [49]
In the citing paper
“Blewett and colleagues (2016) demonstrated that dimethyl fumarate (DMF), a potent electrophile which is currently used to treat psoriasis and relapse-remitting MS, but not MMF inhibited the activation of human and mouse T cells 49.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [49]
In the citing paper
“Mechanistically, DMF blocked the association of PKCθ with the costimulatory receptor CD28 and T cell activation.”
From Coupling Krebs cycle metabolites to signalling in immunity and cancer (2018) · cites this paper as [49]
Citations
Cites
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040
ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS
Allfrey, V. G., Faulkner, R. D., & Mirsky, A. E. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.5.786 · Cited by 2,788
Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902
Self-citationSirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429
Multivalent engagement of chromatin modifications by linked binding modules
Ruthenburg, A. J., Li, H., Patel, D. J., & Allis, C. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2298 · Cited by 1,039
Identification of lysine succinylation as a new post-translational modification
Zhang, Z., Tan, M., Xie, Z., Dai, L., Chen, Y., & Zhao, Y. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.495 · Cited by 1,027
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
Park, J., Chen, Y., Tishkoff, D. X., Peng, C., Tan, M., Dai, L., Xie, Z., Zhang, Y., Zwaans, B. M. M., Skinner, M. E., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.001 · Cited by 1,000
Post-translational modifications in signal integration
Deribe, Y. L., Pawson, T., & Dikic, I. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1842 · Cited by 876
Pandey, R. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf660 · Cited by 783
Weinert, B. T., Scholz, C. W., Wagner, S., Iešmantavičius, V., Su, D., Daniel, J. A., & Choudhary, C. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.07.024 · Cited by 774
Cited by
Sorted by citations
Coupling Krebs cycle metabolites to signalling in immunity and cancer
Ryan, D. G., Murphy, M. P., Frezza, C., Prag, H. A., Chouchani, E. T., O’Neill, L. A., & Mills, E. L. (2018) · Nature Metabolism · doi:10.1038/s42255-018-0014-7 · Cited by 398
Succinylation Links Metabolism to Protein Functions
Yang, Y., & Gibson, G. E. (2019) · Neurochemical Research · doi:10.1007/s11064-019-02780-x · Cited by 231
Peroxiredoxins and Redox Signaling in Plants
Liebthal, M. F., Maynard, D., & Dietz, K. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7164 · Cited by 216
Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis
Hartl, M., Füßl, M., Boersema, P. J., Jost, J. O., Kramer, K., Bakirbas, A., Sindlinger, J., Plöchinger, M., Leister, D., Uhrig, R. G., et al. (2017) · Molecular Systems Biology · doi:10.15252/msb.20177819 · Cited by 162
The Plant PTM Viewer, a central resource for exploring plant protein modifications.
Willems, P., Horne, A., van Parys, T., Goormachtig, S., Smet, I. D., Botzki, A., Breusegem, F. V., & Gevaert, K. (2019) · The Plant Journal · doi:10.1111/tpj.14345 · Cited by 98
Metadata
- Authors
- He, D., Wang, Q., Li, M., Damaris, R. N., Yi, X., Cheng, Z., & Yang, P.
- Affiliations
- Chinese Academy of Sciences (CN)
- Jingjie PTM Biolabs (Hangzhou) Co. Ltd., Hangzhou 310018, China
- Corresponding author
- Yang, Pingfang
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2016-01-28
- Volume
- 15
- Issue
- 3
- Pages
- 879-890
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W2235305215
- Cited by
- 124
- References
- 58
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 7 · 2023: 4 · 2022: 17 · 2021: 14 · 2020: 12 · 2019: 18 · 2018: 12 · 2017: 22 · 2016: 9
- FWCI
- 23.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Proteome Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (31101213, 31271805)
- Chinese Academy of Sciences
- Central People's Government of the People's Republic of China (SAJC201324)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Seed Germination and Physiology
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- lysine acetylation, lysine succinylation, post-translational modification, rice seed germination, seed embryo, metabolic regulation, acetyl-CoA metabolism, glycolysis/gluconeogenesis
- MeSH terms
- Acetylation, Amino Acid Sequence, Lysine, Plant Proteins, Protein Processing, Post-Translational, Oryza, Seeds, Germination, Succinic Acid, Proteome, Amino Acid Motifs, Seedlings, Metabolic Networks and Pathways, Protein Interaction Maps, Gene Ontology
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review