PodcastPosttranslational Modifications

Science Signaling Podcast for 30 August 2016: Human arginine methylome

Sci. Signal.  30 Aug 2016:
Vol. 9, Issue 443, pp. pc18
DOI: 10.1126/scisignal.aai8136

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Abstract

This Podcast features an interview with Michael Nielsen, author of a Research Resource that appears in the 30 August 2016 issue of Science Signaling, about the human arginine methylome. Proteins can be posttranslationally modified by the covalent attachment of methyl groups to arginine or lysine residues. Whereas lysine methylation of histone proteins is important for controlling chromatin dynamics and has been extensively characterized, less is known about arginine methylation. Larsen et al. cataloged arginine methylation sites in the human proteome and found that proteins involved in diverse cellular processes were methylated. Arginine methylation sites colocalized with phosphorylation sites and were hotspots for mutations associated with disease. Arginine methylation was particularly prominent in RNA-binding proteins, and different arginine methyltransferases targeted distinct sets of substrates to control the localization or function of these target proteins. Further analysis and application of this data set will contribute to a more comprehensive understanding of the extent, function, and regulation of protein arginine methylation.

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