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Growing with the wind : Ribosomal protein hydroxylation and cell growth
Authors:Maximiliano J Katz  Julieta M Acevedo  Pablo Wappner
Affiliation:1.Instituto Leloir; Buenos Aires, Argentina;2.German Cancer Research Center (DKFZ); Heidelberg, Germany;3.Consejo Nacional de Investigaciones Científicas y Técnicas; Buenos Aires, Argentina;4.Departamento de Fisiología, Biología Molecular, y Celular; Facultad de Ciencias Exactas y Naturales; Universidad de Buenos Aires; Buenos Aires, Argentina
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   ribosomal oxygenase   ribosomal protein   stop codon read-through   cell growth
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