Growing with the wind. Ribosomal protein hydroxylation and cell growth

Fly (Austin). 2014;8(3):153-6. doi: 10.4161/fly.29943. Epub 2014 Oct 31.

Abstract

In this Extra View we comment on our recent work on Sudestada1 (Sud1), a Drosophila 2-oxoglutarate (2OG)-dependent dioxygenase that belongs to the Ribosomal Oxygenase (ROX) subfamily. Sud1 is required for normal growth in Drosophila, and is conserved in yeast and mammals. We reported that Sud1 hydroxylates the ribosomal protein S23 (RPS23), and that its loss of function restricts growth and provokes activation of the unfolded protein response, apoptosis and autophagy. In this Extra View we speculate on the role that RPS23 hydroxylation might play in stop codon recognition and on the possible link between Sud1 loss-of-function and activation of the Unfolded Protein Response, Stress Granules formation and growth impairment.

Keywords: Drosophila; cell growth; ribosomal oxygenase; ribosomal protein; stop codon read-through.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Cell Growth Processes*
  • Drosophila / enzymology*
  • Drosophila Proteins / metabolism*
  • Gene Expression Regulation*
  • Hydroxylation
  • Prolyl Hydroxylases / metabolism*
  • Ribosomal Proteins / metabolism*

Substances

  • Drosophila Proteins
  • Ribosomal Proteins
  • ribosomal protein S23, Drosophila
  • Prolyl Hydroxylases
  • sud1 protein, Drosophila