LSD2/KDM1B and its cofactor NPAC/GLYR1 endow a structural and molecular model for regulation of H3K4 demethylation.

@article{Fang2013LSD2KDM1BAI,
  title={LSD2/KDM1B and its cofactor NPAC/GLYR1 endow a structural and molecular model for regulation of H3K4 demethylation.},
  author={R Yi-Ping Fang and Fei Chen and Zhenghong Dong and Di Hu and Andrew J. Barbera and Erin A Clark and Jian Fang and Ying Yang and Pinchao Mei and Michael Scott Rutenberg and Ze Li and Ying Zhang and Youwei Xu and Huirong Yang and Ping Wang and Matthew D Simon and Qiongjie Zhou and Jing Li and Mark P. Marynick and Xiaotian Li and Haojie Lu and Ursula Brigitte Kaiser and Robert E. Kingston and Yanhui Xu and Yujiang Geno Shi},
  journal={Molecular cell},
  year={2013},
  volume={49 3},
  pages={558-70}
}
Dynamic regulation of histone methylation represents a fundamental epigenetic mechanism underlying eukaryotic gene regulation, yet little is known about how the catalytic activities of histone demethylases are regulated. Here, we identify and characterize NPAC/GLYR1 as an LSD2/KDM1b-specific cofactor that stimulates H3K4me1 and H3K4me2 demethylation. We determine the crystal structures of LSD2 alone and LSD2 in complex with the NPAC linker region in the absence or presence of histone H3 peptide… CONTINUE READING
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