2019
DOI: 10.1002/1873-3468.13337
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The histone demethylase PHF8 facilitates alternative splicing of the histocompatibility antigen HLA‐G

Abstract: Histone3‐lysine9 (H3K9) residues not only control gene expression, but also contribute to RNA splicing. Here, the H3K9 histone demethylase PHF8 was investigated in endothelial cells for its involvement in alternative splicing. An angiogenic sprouting assay shows the importance of PHF8 for endothelial cells. Immunoprecipitation reveals that PHF8 interacts with U1 spliceosomal proteins, such as SRPK1 and snRNP70. We identify the histocompatibility antigen HLA‐G as a target of PHF8. The inclusion of HLA‐G intron … Show more

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Cited by 6 publications
(5 citation statements)
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“…Histone methylation is important in chromatin packaging and gene expression and has been proven to be involved in the regulation of inflammatory processes and osteogenic differentiation 24,25 . As a histone demethylase, PHF8 regulates the methylation states of various histone lysine residues, thus modulating gene expression 26 . PHF8 also mediates inflammatory processes 15 and plays an important role in the development of craniomaxillofacial bone by regulating the methylation of histone sites H4K20 and H3K9 10 .…”
Section: Discussionmentioning
confidence: 99%
“…Histone methylation is important in chromatin packaging and gene expression and has been proven to be involved in the regulation of inflammatory processes and osteogenic differentiation 24,25 . As a histone demethylase, PHF8 regulates the methylation states of various histone lysine residues, thus modulating gene expression 26 . PHF8 also mediates inflammatory processes 15 and plays an important role in the development of craniomaxillofacial bone by regulating the methylation of histone sites H4K20 and H3K9 10 .…”
Section: Discussionmentioning
confidence: 99%
“…However, unlike other HLA Class I molecules incapable of producing soluble isoforms, it is still unknown why a premature stop codon, located in intron 4 of the HLA-G gene, is matured in EVTs only leading to create soluble HLA-G isoforms. According to the recent study [29], depletion of PHF 8 (Plant Homeodomain Finger protein 8), a histone demethylase of H3K9 (lysine residue 9 on histone H3), in HUVECs (Human umbilical vein endothelial cells) and JEG3 cells, led to increased H3K9me2 (dimethylated state of H3K9) levels within intron 4 of the HLA-G gene. Consequently, the stop codon located in intron 4 of the HLA-G gene is matured to terminate the transcription process, increasing the expression of soluble HLA-G5/6 mRNAs containing intron 4.…”
Section: Progesterone Induced By In-vivo Like Temperature Change Mamentioning
confidence: 99%
“…Histone methyltransferases and demethylases allow the activation of the promoter (H3 4-trimethyl lysine), enhancer activity (H3K4me1), or repression (H3K9me2 / 3, H3K27me2 / 3) [35]. The catalytic role of KDM7 members in the demethylation of repressive histone markers such as H3K9me1 / 2, H3K27me1 / 2, or H4K20me1 is characterized by marked differences in substrate specificity between different enzymes [36,37].…”
Section: Discussionmentioning
confidence: 99%