PHD finger protein 8 is a
protein that in humans is encoded by the PHF8gene.[5]
Function
PHF8 belongs to the family of ferrous iron and
alpha-ketoglutarate-dependent hydroxylases superfamily.,[6] and is active as a
histone lysine demethylase with selectivity for the di-and monomethyl states.[7] PHF8 induces an EMT (epithelial to mesenchymal transition)-like process by upregulating key EMT transcription factors SNAI1 and ZEB1.
Regulation during differentiation
PHF8 was found to be expressional increased during endothelial differentiation and significantly decreased during cardial differentiation of murine embryonic stem cells.[8]
This catalytic activity is disrupted by clinically known mutations to PHF8, which were found to cluster in its catalytic JmjC domain. The F279S mutation of PHF8, found in 2 Finnish brothers with mild
intellectual disability, facial
dysmorphism and
cleft lip/palate,[14] was found to additionally prevent
nuclear localisation of PHF8 overexpressed in human cells.[7]
^
abKoivisto AM, Ala-Mello S, Lemmelä S, Komu HA, Rautio J, Järvelä I (Aug 2007). "Screening of mutations in the PHF8 gene and identification of a novel mutation in a Finnish family with XLMR and cleft lip/cleft palate". Clinical Genetics. 72 (2): 145–9.
doi:
10.1111/j.1399-0004.2007.00836.x.
PMID17661819.
S2CID23326755.
^Qiao Y, Liu X, Harvard C, Hildebrand MJ, Rajcan-Separovic E, Holden JJ, Lewis ME (Aug 2008). "Autism-associated familial microdeletion of Xp11.22". Clinical Genetics. 74 (2): 134–44.
doi:
10.1111/j.1399-0004.2008.01028.x.
PMID18498374.
S2CID22008997.
^Hurst JA, Houlston RS, Roberts A, Gould SJ, Tingey WG (Oct 1995). "Transverse limb deficiency, facial clefting and hypoxic renal damage: an association with treatment of maternal hypertension?". Clinical Dysmorphology. 4 (4): 359–63.
doi:
10.1097/00019605-199510000-00013.
PMID8574428.
S2CID6330050.