Human PAD4 Regulates Histone Arginine Methylation Levels via Demethylimination
University of Southern California · University of California, Los Angeles · +3 more institutions
Abstract
Methylation of arginine (Arg) and lysine residues in histones has been correlated with epigenetic forms of gene regulation. Although histone methyltransferases are known, enzymes that demethylate histones have not been identified. Here, we demonstrate that human peptidylarginine deiminase 4 (PAD4) regulates histone Arg methylation by converting methyl-Arg to citrulline and releasing methylamine. PAD4 targets multiple sites in histones H3 and H4, including those sites methylated by coactivators CARM1 (H3 Arg17) and PRMT1 (H4 Arg3). A decrease of histone Arg methylation, with a concomitant increase of citrullination, requires PAD4 activity in human HL-60 granulocytes. Moreover, PAD4 activity is linked with the…
Citation impact
- FWCI
- 25.31
- Percentile
- 100%
- References
- 29
Authors
15- YWYanming Wang
University of Southern California, University of California, Los Angeles, Baylor College of Medicine, Cornell University, Rockefeller University
- JWJoanna Wysocka
University of Southern California, University of California, Los Angeles, Baylor College of Medicine, Cornell University, Rockefeller University
- JSJoyce Sayegh
University of Southern California, University of California, Los Angeles, Baylor College of Medicine, Cornell University, Rockefeller University
- YLYoung‐Ho Lee
University of Southern California, University of California, Los Angeles, Baylor College of Medicine, Cornell University, Rockefeller University
- JRJulie R. Perlin
University of Southern California, University of California, Los Angeles, Baylor College of Medicine, Cornell University, Rockefeller University
Topics & keywords
- Histone methyltransferase
- Histone
- Methylation
- Histone methylation
- Histone H3
- Citrullination
- Epigenetics
- Histone H4