Deciphering arginine methylation: Tudor tells the tale View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2011-10

AUTHORS

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

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. More... »

PAGES

629

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nrm3185

    DOI

    http://dx.doi.org/10.1038/nrm3185

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1026208293

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/21915143


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