The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Lysine methylation of the NF-κB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-κB signaling
Open accessAbstract
Signaling via the methylation of lysine residues in proteins has been linked to diverse biological and disease processes, yet the catalytic activity and substrate specificity of many human protein lysine methyltransferases (PKMTs) are unknown. We screened over 40 candidate PKMTs and identified SETD6 as a methyltransferase that monomethylated chromatin-associated transcription factor NF-κB subunit RelA at Lys310 (RelAK310me1). SETD6-mediated methylation rendered RelA inert and attenuated RelA-driven transcriptional programs, including inflammatory responses in primary immune cells. RelAK310me1 was recognized by the ankryin repeat of the histone methyltransferase GLP, which under basal conditions promoted a repressed chromatin state at RelA target genes through GLP-mediated methylation of histone H3 Lys9 (H3K9). NF-κB-activation–linked phosphorylation of RelA at Ser311 by protein kinase C-ζ (PKC-ζ) blocked the binding of GLP to RelAK310me1 and relieved repression of the target gene. Our findings establish a previously uncharacterized mechanism by which chromatin signaling regulates inflammation programs.
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Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883 · cited 1×
“1968" language="eng" relation="no"> Chromatin dynamics regulate key cellular functions that influence survival, growth and proliferation, and disruption of chromatin homeostasis has been linked to diverse pathologic processe”
SIRT6 is a histone H3 lysine 9 deacetylase that modulates telomeric chromatin
Michishita, E., McCord, R. A., Berber, E., Kioi, M., Padilla-Nash, H., Damian, M., Cheung, P., Kusumoto, R., Kawahara, T. L. A., Barrett, J. C., et al. (2008) · Nature · doi:10.1038/nature06736 · Cited by 1,111
Self-citationTachibana, M., Sugimoto, K., Fukushima, T., & Shinkai, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101914200 · Cited by 784
Perkins, N. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209937 · Cited by 674
Cited by
The Regulation of NF-κB Subunits by Phosphorylation
Christian, F., Smith, E., & Carmody, R. (2016) · Cells · doi:10.3390/cells5010012 · Cited by 717
Cao, X. (2016) · Nature Reviews Immunology · doi:10.1038/nri.2015.8 · Cited by 665
535 East 70th Street, C. R. B., Goldring, M., Otero, M., Plumb, D., Dragomir, C., Favero, M., EI Hachem, K., Hashimoto, K., Roach, H., Olivotto, E., et al. (2011) · European Cells and Materials · doi:10.22203/ecm.v021a16 · Cited by 489
Non-histone protein methylation as a regulator of cellular signalling and function
Biggar, K. K., & Li, S. S.-C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3915 · Cited by 479
Critical roles of non-histone protein lysine methylation in human tumorigenesis
Hamamoto, R., Saloura, V., & Nakamura, Y. (2015) · Nature Reviews Cancer · doi:10.1038/nrc3884 · Cited by 376
Metadata
- Authors
- Levy, D., Kuo, A. J., Chang, Y., Schaefer, U., Kitson, C., Cheung, P., Espejo, A., Zee, B. M., Liu, C. L., Tangsombatvisit, S., Tennen, R. I., Kuo, A. Y., Tanjing, S., Cheung, R., Chua, K. F., Utz, P. J., Shi, X., Prinjha, R. K., Lee, K., Garcia, B. A., Bedford, M. T., Tarakhovsky, A., Cheng, X., & Gozani, O.
- Venue
- Nature Immunology
- Published
- 2010-12-05
- Volume
- 12
- Issue
- 1
- Pages
- 29-36
- ISSN
- 1529-2908 (ISSN-L)
- 1529-2916
- OpenAlex
- W2167686653
- Cited by
- 255
- References
- 4
- FWCI
- 5.96
- Type
- journal article
- Language
- en
- Open access
- green
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- The paper
- Levy, D., Kuo, A. J., Chang, Y., Schaefer, U., Kitson, C., Cheung, P., Espejo, A., Zee, B. M., Liu, C. L., Tangsombatvisit, S., Tennen, R. I., Kuo, A. Y., Tanjing, S., Cheung, R., Chua, K. F., Utz, P. J., Shi, X., Prinjha, R. K., Lee, K., . . . Gozani, O. (2011). Lysine methylation of the NF-κB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-κB signaling. Nature Immunology. https://doi.org/10.1038/ni.1968
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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