Methylation, a new epigenetic mark for protein stability

Xiao Dong Yang, Acacia Lamb, Lin-Feng Chen

Research output: Contribution to journalReview article

Abstract

Recent studies on the lysine methylation of histones have moved rapidly thanks to the discoveries of a variety of histone lysine methyltransferases. Histone lysine methylation is known to either activate or repress gene expression depending upon the position and status of the methylated lysine residue. Recently, an increasing number of lysine methyltransferases have been identified to modify non-histone proteins. Among those enzymes, the most extensively studied is Set9, a SET domaincontaining lysine methyltransferase. Set9 was initially found to target histone H3 lysine 4 for monomethylation and was subsequently shown to target a variety of non-histone proteins, especially transcription-related factors. Functional studies revealed that Set9-mediated methylation of different non-histone proteins leads to distinct biological consequences, most of which point to protein stability. Here we summarize the latest findings on the effects of Set9-mediated lysine methylation on the stability of non-histone proteins.

Original languageEnglish (US)
Pages (from-to)429-433
Number of pages5
JournalEpigenetics
Volume4
Issue number7
DOIs
StatePublished - Oct 1 2009

Fingerprint

Protein Stability
Epigenomics
Methylation
Lysine
Histones
Methyltransferases
Histone-Lysine N-Methyltransferase
Proteins
Transcription Factors
Gene Expression
Enzymes

Keywords

  • E3 ligase
  • Lysine methylation
  • Non-histone proteins
  • Protein stability
  • Set9

ASJC Scopus subject areas

  • Molecular Biology
  • Cancer Research

Cite this

Methylation, a new epigenetic mark for protein stability. / Yang, Xiao Dong; Lamb, Acacia; Chen, Lin-Feng.

In: Epigenetics, Vol. 4, No. 7, 01.10.2009, p. 429-433.

Research output: Contribution to journalReview article

Yang, Xiao Dong ; Lamb, Acacia ; Chen, Lin-Feng. / Methylation, a new epigenetic mark for protein stability. In: Epigenetics. 2009 ; Vol. 4, No. 7. pp. 429-433.
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