The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Human PAD4 Regulates Histone Arginine Methylation Levels via Demethylimination
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 Arg 17 ) and PRMT1 (H4 Arg 3 ). 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 transcriptional regulation of estrogen-responsive genes in MCF-7 cells. These data suggest that PAD4 mediates gene expression by regulating Arg methylation and citrullination in histones.
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Citations
Cites
Histone acetylation in chromatin structure and transcription
Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884
Cited by
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
“In addition, in vivo data demonstrate that mono- (but not di-) methylated arginines can be deiminated (Wang et al., 2004a).”
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012
Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
Shi, Y., Lan, F., Matson, C., Mulligan, P., Whetstine, J. R., Cole, P. A., Casero, R. A., & Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.12.012 · Cited by 4,051
Neutrophil extracellular traps in immunity and disease
Papayannopoulos, V. (2018) · Nature Reviews Immunology · doi:10.1038/nri.2017.105 · Cited by 3,397
Histone methylation: a dynamic mark in health, disease and inheritance
Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241
Metadata
- Authors
- Wang, Y., Wysocka, J., Sayegh, J., Lee, Y.-H., Perlin, J. R., Leonelli, L., Sonbuchner, L. S., McDonald, C. H., Cook, R. G., Dou, Y., Roeder, R. G., Clarke, S., Stallcup, M. R., Allis, C. D., & Coonrod, S. A.
- Venue
- Science
- Published
- 2004-10-08
- Volume
- 306
- Issue
- 5694
- Pages
- 279-283
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2139610636
- Cited by
- 1,010
- References
- 1
- FWCI
- 22.74
- Type
- journal article
- Language
- en
- Open access
- closed
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- Wang, Y., Wysocka, J., Sayegh, J., Lee, Y.-H., Perlin, J. R., Leonelli, L., Sonbuchner, L. S., McDonald, C. H., Cook, R. G., Dou, Y., Roeder, R. G., Clarke, S., Stallcup, M. R., Allis, C. D., & Coonrod, S. A. (2004). Human PAD4 Regulates Histone Arginine Methylation Levels via Demethylimination. Science. https://doi.org/10.1126/science.1101400
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