SET for life: Biochemical activities and biological functions of SET domain-containing proteins

Hans Martin Herz, Alexander Garruss, Ali Shilatifard*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

240 Scopus citations

Abstract

SET domain-containing proteins belong to a group of enzymes named after a common domain that utilizes the cofactor S-adenosyl-. l-methionine (SAM) to achieve methylation of its substrates. Many SET domain-containing proteins have been shown to display catalytic activity towards particular lysine residues on histones, but emerging evidence also indicates that various non-histone proteins are specifically targeted by this clade of enzymes. Here, we summarize the most recent findings on the biological functions of the major families of SET domain-containing proteins catalyzing the methylation of histones 3 on lysines 4, 9, 27, and 36 (H3K4, H3K9, H3K27, and H3K36) and histone 4 on lysine 20 (H4K20), as well as enzymes that have been reported to modify non-histone substrates.

Original languageEnglish (US)
Pages (from-to)621-639
Number of pages19
JournalTrends in Biochemical Sciences
Volume38
Issue number12
DOIs
StatePublished - Dec 2013

Funding

We thank Drs Edwin Smith and Marc Morgan for insightful discussions and for the critical reading of this manuscript, and Lisa Kennedy for editorial assistance. Studies in Shilatifard's laboratory regarding the subject of this review are supported in part by funding through National Institutes of Health grants R01CA150265, R01CA89455, and R01GM069905 to A.S.

Keywords

  • Histone lysine methylation
  • Non-histone substrates
  • SET domain-containing proteins

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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