Protein arginine methylation of non-histone proteins and its role in diseases

Han Wei, Rasika Mundade, Kevin C. Lange, Tao Lu

Research output: Contribution to journalArticle

83 Citations (Scopus)

Abstract

Protein arginine methyltransferases (PRMTs) are a family of enzymes that can methylate arginine residues on histones and other proteins. PRMTs play a crucial role in influencing various cellular functions, including cellular development and tumorigenesis. Arginine methylation by PRMTs is found on both nuclear and cytoplasmic proteins. Recently, there is increasing evidence regarding post-translational modifications of non-histone proteins by PRMTs, illustrating the previously unknown importance of PRMTs in the regulation of various cellular functions by post-translational modifications. In this review, we present the recent developments in the regulation of non-histone proteins by PRMTs.

Original languageEnglish
Pages (from-to)32-41
Number of pages10
JournalCell Cycle
Volume13
Issue number1
DOIs
StatePublished - Jan 1 2014

Fingerprint

Protein-Arginine N-Methyltransferases
Methylation
Arginine
Proteins
Post Translational Protein Processing
Nuclear Proteins
Histones
Carcinogenesis
Enzymes

Keywords

  • Arginine
  • Post-translational modification
  • Protein arginine methyltransferases

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Developmental Biology

Cite this

Protein arginine methylation of non-histone proteins and its role in diseases. / Wei, Han; Mundade, Rasika; Lange, Kevin C.; Lu, Tao.

In: Cell Cycle, Vol. 13, No. 1, 01.01.2014, p. 32-41.

Research output: Contribution to journalArticle

Wei, Han ; Mundade, Rasika ; Lange, Kevin C. ; Lu, Tao. / Protein arginine methylation of non-histone proteins and its role in diseases. In: Cell Cycle. 2014 ; Vol. 13, No. 1. pp. 32-41.
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