title: Intersection of selenoproteins and kinase signalling.
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).
authors.affiliation: Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland.
authors.forename: Anna
authors.initials: A
authors.lastname: Lenart
authors.forename: Krzysztof
authors.initials: K
authors.lastname: Pawłowski
mesh_terms: D001665:Binding Sites / Q000235:genetics; D006801:Humans; D008958:Models, Molecular; D009135:Muscular Diseases / Q000235:genetics / Q000378:metabolism; D009154:Mutation; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D051140:Selenoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction; D013879:Thioredoxins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D051140:Selenoproteins; D013879:Thioredoxins; D011494:Protein Kinases