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 language | English (US) |
|---|---|
| Pages (from-to) | 629-642 |
| Number of pages | 14 |
| Journal | Nature Reviews Molecular Cell Biology |
| Volume | 12 |
| Issue number | 10 |
| DOIs | |
| State | Published - Oct 2011 |
Funding
We dedicate this paper to Maggie Pawson, in memory of her many contributions to the world of signal transduction. We thank J. Park for assistance with the figures and B. Liu, G. Gish and J. Min for comments on the manuscript. C.C. and J.J. are recipients of fellowships from the Canadian Institutes for Health Research (CIHR). Work in the laboratory of T.P. is supported by grants from the CIHR, the Canadian Cancer Society, Genome Canada through the Ontario Genomics Institute and the Ontario Research Fund.
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology