Intersection of selenoproteins and kinase signalling

Biochim Biophys Acta. 2013 Jul;1834(7):1279-84. doi: 10.1016/j.bbapap.2013.03.019. Epub 2013 Mar 27.

Abstract

The small, obscure group of selenoprotein oxidoreductases and the huge clan of kinases, the workhorses of cellular signalling, are rarely discussed together. Focusing on selenoproteins of unknown structures, we predict a thioredoxin-like fold for the Selenoprotein N (SelN) family and use the structure to rationalise effects of the muscular myopathy-linked mutations in the gene coding SelN. Discussing the recent prediction of a protein kinase-like domain in the Selenoprotein O (SelO), we reiterate evidence for an oxidoreductase function alongside the predicted kinase domain. Thus, we propose that SelO, the strongly conserved kinase-cum-tentative-oxidoreductase may reflect oxidoreductase regulation of kinase networks. Also, we use bibliometric and systems biology approach to explore the kinase-selenoprotein relationships that begin to emerge from the literature. This article is part of a Special Issue entitled: Inhibitors of Protein Kinases (2012).

Publication types

  • Review

MeSH terms

  • Binding Sites / genetics
  • Humans
  • Models, Molecular
  • Muscular Diseases / genetics
  • Muscular Diseases / metabolism
  • Mutation
  • Protein Kinases / chemistry
  • Protein Kinases / genetics
  • Protein Kinases / metabolism*
  • Protein Structure, Tertiary
  • Selenoproteins / chemistry
  • Selenoproteins / genetics
  • Selenoproteins / metabolism*
  • Signal Transduction*
  • Thioredoxins / chemistry
  • Thioredoxins / genetics
  • Thioredoxins / metabolism

Substances

  • Selenoproteins
  • Thioredoxins
  • Protein Kinases