ArticleMolecular bioSystems2011
Discovery of peptidylarginine deiminase-4 substrates by protein array: antagonistic citrullination and methylation of human ribosomal protein S2.
Article in Molecular bioSystems, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 57 citations in OpenAlex.
- A quantitative and site-specific atlas of the citrullinome reveals widespread existence of citrullination and insights into PADI4 substrates.Nature structural & molecular biology · 2024Article
- The Role of Citrullination Modification in CD4Biomolecules · 2024Review
- Investigating the Precise Identification of Citrullination Sites with High- Performance Score Metrics Using a Powerful Computation Predicting Tool.Combinatorial chemistry & high throughput screening · 2024Article
- Investigating the cell membrane localization of PADI4 in breast cancer cells and inhibition of anti-PADI4 monoclonal antibody.Journal of cancer research and clinical oncology · 2023Article
- Citrullination and the protein code: crosstalk between post-translational modifications in cancer.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Review
- Trim28 citrullination maintains mouse embryonic stem cell pluripotency via regulating Nanog and Klf4 transcription.Science China. Life sciences · 2023Article
- PAD4 and Its Inhibitors in Cancer Progression and Prognosis.Pharmaceutics · 2022Review
- Citrullination in the pathology of inflammatory and autoimmune disorders: recent advances and future perspectives.Cellular and molecular life sciences : CMLS · 2022Review
- Extracellular DNA Traps: Origin, Function and Implications for Anti-Cancer Therapies.Frontiers in oncology · 2022Review
- Cellular pathways influenced by protein arginine methylation: Implications for cancer.Molecular cell · 2021Review
- Extracellular Vesicle Signatures and Post-Translational Protein Deimination in Purple Sea Urchin (Biology · 2021Article
- PAD4 takes charge during neutrophil activation: Impact of PAD4 mediated NET formation on immune-mediated disease.Journal of thrombosis and haemostasis : JTH · 2021Review
- Histone citrullination: a new target for tumors.Molecular cancer · 2021Review
- Early and Late Processes Driving NET Formation, and the Autocrine/Paracrine Role of Endogenous RAGE Ligands.Frontiers in immunology · 2021Article
- PAD enzymes in rheumatoid arthritis: pathogenic effectors and autoimmune targets.Nature reviews. Rheumatology · 2020Review
- Peptidylarginine Deiminase Inhibitors Reduce Bacterial Membrane Vesicle Release and Sensitize Bacteria to Antibiotic Treatment.Frontiers in cellular and infection microbiology · 2019Article
- Article
- DNA Methylation: a New Player in Multiple Sclerosis.Molecular neurobiology · 2017Review
- Emerging Role for Methylation in Multiple Sclerosis: Beyond DNA.Trends in molecular medicine · 2017Review
- Epitope Specificity of Anti-Citrullinated Protein Antibodies.Antibodies (Basel, Switzerland) · 2017Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Peptidylarginine deiminase (PAD) catalyzes the posttranslational citrullination of selected proteins in a calcium dependent manner. The PAD4 isoform has been implicated in multiple sclerosis, rheumatoid arthritis, some types of cancer, and plays a role in gene regulation. However, the substrate selectivity of PAD4 is not well defined, nor is the impact of citrullination on many other pathways. Here, a high-density protein array is used as a primary screen to identify 40 previously unreported PAD4 substrates, 10 of which are selected and verified in a cell lysate-based secondary assay. One of the most prominent hits, human 40S ribosomal protein S2 (RPS2), is characterized in detail. PAD4 citrullinates the Arg-Gly repeat region of RPS2, which is also an established site for Arg methylation by protein arginine methyltransferase 3 (PRMT3). As in other systems, crosstalk is observed; citrullination and methylation modifications are found to be antagonistic to each other, suggesting a conserved posttranslational regulatory strategy. Both PAD4 and PRMT3 are found to co-sediment with the free 40S ribosomal subunit fraction from cell extracts. These findings are consistent with participation of citrullination in the regulation of RPS2 and ribosome assembly. This application of protein arrays to reveal new PAD4 substrates suggests a role for citrullination in a number of different cellular pathways.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.