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

Biochim Biophys Acta Rev Cancer

Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Cancer Center of Renmin Hospital of Wuhan University, Wuhan University, Wuhan 430072, China. Electronic address:

Published: January 2021

AI Article Synopsis

  • SETD3 is a unique protein in the SET-domain family, recognized as the first known histidine methyltransferase in animals, specifically targeting histidine 73 (His73) on actin.
  • This review highlights recent findings about SETD3, including its structure, how it recognizes substrates, and its roles in physiological processes.
  • The paper discusses the potential links between SETD3 and human cancers, raising questions to encourage further exploration of this newly identified enzyme's significance.

Article 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.

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Source
http://dx.doi.org/10.1016/j.bbcan.2020.188465DOI Listing

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