The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Nuclear Localization of Peptidylarginine Deiminase V and Histone Deimination in Granulocytes
Open accessAbstract
Peptidylarginine deiminase (PAD) deiminates arginine residues in proteins to citrulline residues Ca(2+) dependently. There are four types of PADs, I, II, III, and V, in humans. We studied the subcellular distribution of PAD V in HL-60 granulocytes and peripheral blood granulocytes. Expression of green fluorescent protein-tagged PADs in HeLa cells revealed that PAD V is localized in the nucleus, whereas PAD I, II, and III are localized in the cytoplasm. PAD V deletion mutants indicated that the sequence residues 45-74 have a nuclear localization signal (NLS). A sequence feature of this NLS is a three-lysine residue cluster preceded by a proline residue and is not found in the three other PADs. Substitution of the lysine cluster by an alanine cluster abrogated the nuclear import activity. These results suggested that the NLS is a classical monopartite NLS. HL-60 granulocytes, neutrophils, and eosinophils stained with antibody specific for PAD V exhibited distinct positive signals in the nucleus. Subcellular fractionation of HL-60 granulocytes also showed the nuclear localization of the enzyme. When neutrophils were stimulated with calcium ionophore, protein deimination occurred in the nucleus. The major deiminated proteins were identified as histones H2A, H3, and H4. The implication of PAD V in histone modifications is discussed.
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Cited by
Wang, Y., Li, M., Stadler, S., Correll, S., Li, P., Wang, D., Hayama, R., Leonelli, L., Han, H., Grigoryev, S. A., et al. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200806072 · Cited by 1,521
PAD4 is essential for antibacterial innate immunity mediated by neutrophil extracellular traps
Li, P., Li, M., Lindberg, M. R., Kennett, M. J., Xiong, N., & Wang, Y. (2010) · Journal of Experimental Medicine · doi:10.1084/jem.20100239 · Cited by 1,495
Human PAD4 Regulates Histone Arginine Methylation Levels via Demethylimination
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., et al. (2004) · Science · doi:10.1126/science.1101400 · Cited by 1,010
PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease
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Regulation of histone methylation by demethylimination and demethylation
Klose, R. J., & Zhang, Y. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2143 · Cited by 887
Metadata
- Authors
- Nakashima, K., Hagiwara, T., & Yamada, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-12
- Volume
- 277
- Issue
- 51
- Pages
- 49562-49568
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2057259507
- Cited by
- 379
- References
- 36
- FWCI
- 3.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
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