Histone deacetylase isoforms regulate innate immune responses by deacetylating mitogen‐activated protein kinase phosphatase‐1

@article{Jeong2014HistoneDI,
  title={Histone deacetylase isoforms regulate innate immune responses by deacetylating mitogen‐activated protein kinase phosphatase‐1},
  author={Youngtae Jeong and Ronghui Du and X. Zhu and Shasha Yin and J. Wang and H. Cui and W. Cao and C. Lowenstein},
  journal={Journal of Leukocyte Biology},
  year={2014},
  volume={95}
}
The MAPK pathway mediates TLR signaling during innate immune responses. We discovered previously that MKP‐1 is acetylated, enhancing its interaction with its MAPK substrates and deactivating TLR signaling. As HDACs modulate inflammation by deacetylating histone and nonhistone proteins, we hypothesized that HDACs may regulate LPS‐induced inflammation by deacetylating MKP‐1. We found that mouse macrophages expressed a subset of HDAC isoforms (HDAC1, HDAC2, and HDAC3), which all interacted with… Expand
HDAC1/2‐mediated regulation of JNK and ERK phosphorylation in bovine mammary epithelial cells in response to TNF‐α
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