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Histone lysine demethylase PHF8

Definition:

Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Required for brain development, probably by regulating expression of neuron-specific genes. Only has activity toward H4K20Me1 when nucleosome is used as a substrate and when not histone octamer is used as substrate. May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: has weak activity toward H3K9Me2 in absence of H3K4me3, while it has high activity toward H3K9me2 when binding H3K4me3. Positively modulates transcription of histone demethylase KDM5C, acting synergistically with transcription factor ARX; synergy may be related to enrichment of histone H3K4me3 in regulatory elements.

References:

[1]. Lin Yu, et al. Structural insights into a novel histone demethylase PHF8. Cell Res. 2010 Feb;20(2):166-73. [Content Brief]

[2]. Ziqi Zhu, et al. PHF8 is a histone H3K9me2 demethylase regulating rRNA synthesis. Cell Res. 2010 Jul;20(7):794-801. [Content Brief]

[3]. Wen Liu, et al. PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression. Nature. 2010 Jul 22;466(7305):508-12. [Content Brief]

[4]. Hank H Qi, et al. Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development. Nature. 2010 Jul 22;466(7305):503-7. [Content Brief]

[5]. Klaus Fortschegger, et al. PHF8 targets histone methylation and RNA polymerase II to activate transcription. Mol Cell Biol. 2010 Jul;30(13):3286-98. [Content Brief]

[6]. Jihui Qiu, et al. The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation. Cell Res. 2010 Aug;20(8):908-18. [Content Brief]

[7]. Weijun Feng, et al. PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation. Nat Struct Mol Biol. 2010 Apr;17(4):445-50. [Content Brief]

[8]. John R Horton, et al. Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases. Nat Struct Mol Biol. 2010 Jan;17(1):38-43. [Content Brief]

[9]. Christoph Loenarz, et al. PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nepsilon-dimethyl lysine demethylase. Hum Mol Genet. 2010 Jan 15;19(2):217-22. [Content Brief]

[10]. Daniela Kleine-Kohlbrecher, et al. A functional link between the histone demethylase PHF8 and the transcription factor ZNF711 in X-linked mental retardation. Mol Cell. 2010 Apr 23;38(2):165-78. [Content Brief]

[11]. Loredana Poeta, et al. Histone demethylase KDM5C is a SAHA-sensitive central hub at the crossroads of transcriptional axes involved in multiple neurodevelopmental disorders. Hum Mol Genet. 2019 Dec 15;28(24):4089-4102. [Content Brief]

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