Human PAD4 Regulates Histone Arginine Methylation Levels via Demethylimination

By Yanming Wang, J. Wysocka, Joyce Sayegh, Young-Ho Lee, J. Perlin, L. Leonelli, Lakshmi S. Sonbuchner, Charles H. McDonald, R. Cook, Y. Dou and 5 more. Science, 2004

1,065 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/3c8680779260a740bbbb35e66e95edd704556298

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In Molecular Biology

1. Yi Zhang
2. C. D. Allis
3. Wolf Reik
4. Paul Tempst
5. H. Erdjument‐Bromage
6. Y. Tsukada
7. R. Klose
8. Cyrus Martin

Citations in the corpus

• Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps (2010, background): “Citrullination may account for some of the NE-independent shifts observed in histone H3 during NET formation only in conjunction with additional modifications because deimination has been reported to increase the mobility of these proteins (Wang et al., 2004).”
• PAD4 is essential for antibacterial innate immunity mediated by neutrophil extracellular traps (2010, methodology): “The conversion of histone Arg or monomethyl-Arg to citrulline residues is catalyzed by peptidylarginine deiminase 4 (PAD4; also called PADI4 or PADV; Wang et al., 2004), a neutrophil enriched nuclear enzyme (Nakashima et al., 2002).”
• Epigenetics and gene expression (2010, background): “The action of PAD4 has been best studied in the context of estrogen regulation of pS2 transcription, where PAD4 represses transcription.”
• Thrombosis: tangled up in NETs. (2014, background): “During the hypercitrullination of specific arginine residues on histones H3 andH4, there is a loss of positive charge from the transformed arginine residues, and the linker histone H1 and heterochromatin protein 1b dissociate from the nucleosome structure.(13,14) Overexpression of PAD4 results in ch”
• Histone Modifications and Cancer. (2016, background): “Of the PAD family, only PAD4 has a nuclear localization signal and been clearly shown to deiminate/citrullinate histones H3 (Arg residues 2, 8, 17, 26), H2A, H4 (Arg3), and H1R54 (Wang et al. 2004; Tanikawa et al. 2012; Christophorou et al. 2014), although a recent report showed PAD2 as deiminating ”
• RNA meets chromatin. (2005, background): “Regardless of position or function, these covalent marks can be placed and removed by a variety of site-specific enzymes such as histone acetyltransferases (HATs) and histone deacetylases (HDACs), histone methyltransferases (HMTs), and the newly discovered “demethylating” activities (Cuthbert et al.”
• Histone hypercitrullination mediates chromatin decondensation and neutrophil extracellular trap formation (2009, methodology): “Acid extraction of histones and Western blotting The acid extraction of histones and Western blotting with H4Cit3 (1:2,000; Millipore), H3Cit (1:3,000; Abcam), and H3 (1:3,000; Abcam) antibodies were performed essentially as previously described ( Wang et al., 2004 ).”
• JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor. (2006, methodology): “For protein identifi-cation, the candidate polypeptide was digested with trypsin, and the protein was identified as previously described (Wang et al., 2004a).”
• Metabolic reprogramming and epigenetic modifications on the path to cancer (2021, background): “Among the PAD family members, PAD4 is the only protein with a nuclear localization signal (NLS) and has been reported to citrullinate histone H3 (Arg 2, 8, 17, 26), H2A, H4 (Arg 3), and H1 (Arg 54) (Wang et al., 2004; Tanikawa et al., 2012; Christophorou et al., 2014).”