Non-histone Methylation of SET7/9 and its Biological Functions

Recent Pat Anticancer Drug Discov. 2022;17(3):231-243. doi: 10.2174/1574892816666211202160041.

Abstract

Background: (su(var)-3-9,enhancer-of-zeste,trithorax) domain-containing protein 7/9 (SET7/9) is a member of the protein lysine methyltransferases (PLMTs or PKMTs) family. It contains a SET domain. Recent studies demonstrate that SET7/9 methylates both lysine 4 of histone 3 (H3-K4) and lysine(s) of non-histone proteins, including transcription factors, tumor suppressors, and membrane-associated receptors.

Objective: This article mainly reviews the non-histone methylation effects of SET7/9 and its functions in tumorigenesis and development.

Methods: PubMed was screened for this information.

Results: SET7/9 plays a key regulatory role in various biological processes such as cell proliferation, transcription regulation, cell cycle, protein stability, cardiac morphogenesis, and development. In addition, SET7/9 is involved in the pathogenesis of hair loss, breast cancer progression, human carotid plaque atherosclerosis, chronic kidney disease, diabetes, obesity, ovarian cancer, prostate cancer, hepatocellular carcinoma, and pulmonary fibrosis.

Conclusion: SET7/9 is an important methyltransferase, which can catalyze the methylation of a variety of proteins. Its substrates are closely related to the occurrence and development of tumors.

Keywords: SET7/9; lysine methyltransferase; methylation; non-histone protein; teratoma; tumorigenesis.

Publication types

  • Review

MeSH terms

  • Animals
  • Biological Phenomena
  • Cell Proliferation
  • Histone-Lysine N-Methyltransferase / chemistry
  • Histone-Lysine N-Methyltransferase / metabolism*
  • Histones / chemistry
  • Histones / metabolism
  • Humans
  • Lysine / chemistry
  • Lysine / metabolism
  • Male
  • Methylation

Substances

  • Histones
  • Histone-Lysine N-Methyltransferase
  • SETD7 protein, human
  • Lysine