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WIREs RNA
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A jack of all trades: the RNA ‐binding protein vigilin

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The vigilin family of proteins is evolutionarily conserved from yeast to humans and characterized by the proteins’ 14 or 15 hnRNP K homology (KH) domains, typically associated with RNA‐binding. Vigilin is the largest RNA‐binding protein (RBP) in the KH domain‐containing family and one of the largest RBP known to date. Since its identification 30 years ago, vigilin has been shown to bind over 700 mRNAs and has been associated with cancer progression and cardiovascular disease. We provide a brief historic overview of vigilin research and outline the proteins’ different functions, focusing on maintenance of genome ploidy, heterochromatin formation, RNA export, as well as regulation of translation, mRNA transport, and mRNA stability. The multitude of associated functions is reflected by the large number of identified interaction partners, ranging from tRNAs, mRNAs, ribosomes and ribosome‐associated proteins, to histone methyltransferases and DNA‐dependent protein kinases. Most of these partners bind to vigilin's carboxyterminus, and the two most C‐terminal KH domains of the protein, KH13 and KH14, represent the main mRNA‐binding interface. Since the nuclear functions of vigilins in particular are not conserved, we outline a model for the basal functions of vigilins, as well as those which were acquired during the transition from unicellular organisms to metazoa. WIREs RNA 2017, 8:e1448. doi: 10.1002/wrna.1448

This article is categorized under:

  • RNA Interactions with Proteins and Other Molecules > Protein–RNA Recognition
  • RNA Interactions with Proteins and Other Molecules > Protein–RNA Interactions: Functional Implications
  • Translation > Translation Regulation
Timeline of the identification of vigilin homologs and their functions. (a) Timeline highlighting the years in which the vigilin homologs were identified. (b) A table summarizing the reported localization and functions of the vigilin homologs.
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Models of vigilin functions. Vigilin‐associated complexes are shown in (a) lower eukaryotes (represented by a shmooing S. cerevisiae cell) and in (b) higher eukaryotes (represented by a HeLa cell). Proteins with homologous roles are shown in the middle list. Proteins with roles specific to either lower or higher eukaryotes are listed under the respective cell.
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The domain arrangement of vigilin homologs. (a) Schematics of vigilin homologs are shown with classical KH domains in blue and divergent KH domains in red. All schematics are aligned based on KH1. The vigilins of lower eukaryotes (with only 14 KH domains) are shown at the top. (b) The evolutionary relationship between the various members of the vigilin protein family. The phylogenetic tree is generated based on multiple sequence alignment of the vigilin proteins. Branch length represent amount of genetic change. (c) Schematic of the S. cerevisiae and H. sapiens vigilins highlighting the known vigilin domains which interact with other proteins. Asterisks (*) indicates the KH domains of S. cerevisiae Scp160p with RNA‐contacting amino acids. For more information, see main text.
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RNA Interactions with Proteins and Other Molecules > Protein–RNA Recognition
RNA Interactions with Proteins and Other Molecules > Protein–RNA Interactions: Functional Implications
Translation > Translation Regulation

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