The methyltransferase SETD3-mediated histidine methylation: Biological functions and potential implications in cancers

Biochim Biophys Acta Rev Cancer. 2021 Jan;1875(1):188465. doi: 10.1016/j.bbcan.2020.188465. Epub 2020 Nov 4.

Abstract

SETD3 belongs to a family of SET-domain containing proteins. Recently, SETD3 was found as the first and so-far the only known metazoan histidine methyltransferase that catalyzes actin histidine 73 (His73) methylation, a pervasive modification which was discovered more than 50 years ago. In this review, we summarize some recent advances in SETD3 research, focusing on structural properties, substrate-recognition features, and physiological functions. We particularly highlight potential pathological relevance of SETD3 in human cancers and raise some questions to promote discussion about this novel histidine methyltransferase.

Keywords: Cancers; Functions; Histidine methylation; SETD3; Structure.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actins / genetics
  • Histidine / genetics
  • Histone Methyltransferases / genetics*
  • Histone-Lysine N-Methyltransferase / genetics*
  • Humans
  • Neoplasms / genetics*
  • Neoplasms / pathology
  • Protein Processing, Post-Translational / genetics*

Substances

  • Actins
  • Histidine
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase
  • SETD3 protein, human