Role for tyrosine phosphorylation of SUV39H1 histone methyltransferase in enhanced trimethylation of histone H3K9 via neuregulin-1/ErbB4 nuclear signaling

Nakajo, Haruna; Ishibashi, Keiichiro; Aoyama, Kazumasa; Kubota, Sho; Hasegawa, Hitomi; Yamaguchi, Noritaka; Yamaguchi, Naoto

doi:10.1016/j.bbrc.2019.02.130

Cited by 5 publications

(1 citation statement)

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“…KMT1A, known as SUV39H1, is phosphorylated at residues Tyr297 (mouse Tyr303 and flies Tyr308) by receptor-type tyrosine kinase ERBB4, which enhances the tri-methylation activity of histone H3K9 [ 61 ]. And the protein level of SUV39H1 peaks at the S phase and maintains from S to M phases in the cell cycle, in which SUV39H1 is phosphorylated by CDK2 at Ser391.…”

Section: The Regulation Of Histone Lysine and Arginine Methyltransfer...mentioning

confidence: 99%

The phosphorylation to acetylation/methylation cascade in transcriptional regulation: how kinases regulate transcriptional activities of DNA/histone-modifying enzymes

Zhao

Malik

2022

Cell Biosci

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Transcription factors directly regulate gene expression by recognizing and binding to specific DNA sequences, involving the dynamic alterations of chromatin structure and the formation of a complex with different kinds of cofactors, like DNA/histone modifying-enzymes, chromatin remodeling factors, and cell cycle factors. Despite the significance of transcription factors, it remains unclear to determine how these cofactors are regulated to cooperate with transcription factors, especially DNA/histone modifying-enzymes. It has been known that DNA/histone modifying-enzymes are regulated by post-translational modifications. And the most common and important modification is phosphorylation. Even though various DNA/histone modifying-enzymes have been classified and partly explained how phosphorylated sites of these enzymes function characteristically in recent studies. It still needs to find out the relationship between phosphorylation of these enzymes and the diseases-associated transcriptional regulation. Here this review describes how phosphorylation affects the transcription activity of these enzymes and other functions, including protein stability, subcellular localization, binding to chromatin, and interaction with other proteins.

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Section: The Regulation Of Histone Lysine and Arginine Methyltransfer...mentioning

confidence: 99%