Deciphering arginine methylation: Tudor tells the tale

Chen Chen, Timothy J. Nott, Jing Jin, Tony Pawson*

*Corresponding author for this work

Research output: Contribution to journalReview article

152 Scopus citations

Abstract

Proteins can be modified by post-translational modifications such as phosphorylation, methylation, acetylation and ubiquitylation, creating binding sites for specific protein domains. Methylation has pivotal roles in the formation of complexes that are involved in cellular regulation, including in the generation of small RNAs. Arginine methylation was discovered half a century ago, but the ability of methylarginine sites to serve as binding motifs for members of the Tudor protein family, and the functional significance of the protein-protein interactions that are mediated by Tudor domains, has only recently been appreciated. Tudor proteins are now known to be present in PIWI complexes, where they are thought to interact with methylated PIWI proteins and regulate the PIWI-interacting RNA (piRNA) pathway in the germ line.

Original languageEnglish (US)
Pages (from-to)629-642
Number of pages14
JournalNature Reviews Molecular Cell Biology
Volume12
Issue number10
DOIs
StatePublished - Oct 1 2011

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ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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