Author: Angrisani A1, Matrone N2, Belli V3, Vicidomini R2, Di Maio N2, Turano M2, Scialò F4, Netti PA5, Porcellini A2, Furia M6
Affiliation:
1Department of Biology, University of Naples "Federico II", Complesso Universitario Monte Santangelo, via Cinthia, 80126 Napoli, Italy. Electronic address: alberto.angrisani@unina.it.
2Department of Biology, University of Naples "Federico II", Complesso Universitario Monte Santangelo, via Cinthia, 80126 Napoli, Italy.
3Istituto Italiano di Tecnologia, IIT@CRIB, Largo Barsanti e Matteucci 53, 80125 Napoli, Italy.
4Institute for Cell and Molecular Biosciences, Campus for Ageing and Vitality, University of Newcastle, Newcastle-upon-Tyne NE4 5PL, United Kingdom.
5Istituto Italiano di Tecnologia, IIT@CRIB, Largo Barsanti e Matteucci 53, 80125 Napoli, Italy; Centro di Ricerca Interdipartimentale sui Biomateriali CRIB, Università di Napoli Federico II, Piazzale Tecchio 80, 80125 Napoli, Italy.
6Department of Biology, University of Naples "Federico II", Complesso Universitario Monte Santangelo, via Cinthia, 80126 Napoli, Italy; Centro di Ricerca Interdipartimentale sui Biomateriali CRIB, Università di Napoli Federico II, Piazzale Tecchio 80, 80125 Napoli, Italy. Electronic address: mfuria@unina.it.
Conference/Journal: Redox Biol.
Date published: 2017 Nov 6
Other:
Volume ID: 14 , Pages: 557-565 , Special Notes: doi: 10.1016/j.redox.2017.11.003. [Epub ahead of print] , Word Count: 197
The human DKC1 gene encodes dyskerin, an evolutionarily conserved nuclear protein whose overexpression represents a common trait of many types of aggressive sporadic cancers. As a crucial component of the nuclear H/ACA snoRNP complexes, dyskerin is involved in a variety of essential processes, including telomere maintenance, splicing efficiency, ribosome biogenesis, snoRNAs stabilization and stress response. Although multiple minor dyskerin splicing isoforms have been identified, their functions remain to be defined. Considering that low-abundance splice variants could contribute to the wide functional repertoire attributed to dyskerin, possibly having more specialized tasks or playing significant roles in changing cell status, we investigated in more detail the biological roles of a truncated dyskerin isoform that lacks the C-terminal nuclear localization signal and shows a prevalent cytoplasmic localization. Here we show that this dyskerin variant can boost energy metabolism and improve respiration, ultimately conferring a ROS adaptive response and a growth advantage to cells. These results reveal an unexpected involvement of DKC1 in energy metabolism, highlighting a previously underscored role in the regulation of metabolic cell homeostasis.
Copyright © 2017 The Authors. Published by Elsevier B.V. All rights reserved.
KEYWORDS: DKC1; Energy metabolism; Mitochondria; PRDX-2; ROS signaling
PMID: 29132127 DOI: 10.1016/j.redox.2017.11.003
