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A dynamic link between H/ACA snoRNP components and cytoplasmic stress granules.

Abstract

Many cell stressors block protein translation, inducing formation of cytoplasmic aggregates. These aggregates, named stress granules (SGs), are composed by translationally stalled ribonucleoproteins and their assembly strongly contributes to cell survival. Composition and dynamics of SGs are thus important starting points for identifying critical factors of the stress response. In the present study we link components of the H/ACA snoRNP complexes, highly concentrated in the nucleoli and the Cajal bodies, to SG composition. H/ACA snoRNPs are composed by a core of four highly conserved proteins -dyskerin, Nhp2, Nop10 and Gar1- and are involved in several fundamental processes, including ribosome biogenesis, RNA pseudouridylation, stabilization of small nucleolar RNAs and telomere maintenance. By taking advantage of cells overexpressing a dyskerin splice variant undergoing a dynamic intracellular trafficking, we were able to show that H/ACA snoRNP components can participate in SG formation, this way contributing to the stress response and perhaps transducing signals from the nucleus to the cytoplasm. Collectively, our results show for the first time that H/ACA snoRNP proteins can have additional non-nuclear functions, either independently or interacting with each other, thus further strengthening the close relationship linking nucleolus to SG composition.

Authors+Show Affiliations

Department of Biology, University of Naples "Federico II", Complesso Universitario Monte Santangelo, via Cinthia, 80126 Napoli, Italy.Department of Biology, University of Naples "Federico II", Complesso Universitario Monte Santangelo, via Cinthia, 80126 Napoli, Italy.Department of Biology, University of Naples "Federico II", Complesso Universitario Monte Santangelo, via Cinthia, 80126 Napoli, Italy.Department of Biology, University of Naples "Federico II", Complesso Universitario Monte Santangelo, via Cinthia, 80126 Napoli, Italy.Department of Biology, University of Naples "Federico II", Complesso Universitario Monte Santangelo, via Cinthia, 80126 Napoli, Italy.Department of Biology, University of Naples "Federico II", Complesso Universitario Monte Santangelo, via Cinthia, 80126 Napoli, Italy.Department of Biology, University of Naples "Federico II", Complesso Universitario Monte Santangelo, via Cinthia, 80126 Napoli, Italy.Department of Biology, University of Naples "Federico II", Complesso Universitario Monte Santangelo, via Cinthia, 80126 Napoli, Italy. Electronic address: alberto.angrisani@unina.it.Department of Biology, University of Naples "Federico II", Complesso Universitario Monte Santangelo, via Cinthia, 80126 Napoli, Italy. Electronic address: mfuria@unina.it.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31412274

Citation

Belli, Valentina, et al. "A Dynamic Link Between H/ACA snoRNP Components and Cytoplasmic Stress Granules." Biochimica Et Biophysica Acta. Molecular Cell Research, 2019, p. 118529.
Belli V, Matrone N, Sagliocchi S, et al. A dynamic link between H/ACA snoRNP components and cytoplasmic stress granules. Biochim Biophys Acta Mol Cell Res. 2019.
Belli, V., Matrone, N., Sagliocchi, S., Incarnato, R., Conte, A., Pizzo, E., ... Furia, M. (2019). A dynamic link between H/ACA snoRNP components and cytoplasmic stress granules. Biochimica Et Biophysica Acta. Molecular Cell Research, p. 118529. doi:10.1016/j.bbamcr.2019.118529.
Belli V, et al. A Dynamic Link Between H/ACA snoRNP Components and Cytoplasmic Stress Granules. Biochim Biophys Acta Mol Cell Res. 2019 Aug 11;118529. PubMed PMID: 31412274.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A dynamic link between H/ACA snoRNP components and cytoplasmic stress granules. AU - Belli,Valentina, AU - Matrone,Nunzia, AU - Sagliocchi,Serena, AU - Incarnato,Rosa, AU - Conte,Andrea, AU - Pizzo,Elio, AU - Turano,Mimmo, AU - Angrisani,Alberto, AU - Furia,Maria, Y1 - 2019/08/11/ PY - 2019/01/17/received PY - 2019/07/08/revised PY - 2019/08/05/accepted PY - 2019/8/15/pubmed PY - 2019/8/15/medline PY - 2019/8/15/entrez KW - Dyskerin KW - Nucleolus KW - RNP bodies KW - Ribosome KW - Stress response KW - snoRNPs SP - 118529 EP - 118529 JF - Biochimica et biophysica acta. Molecular cell research JO - Biochim Biophys Acta Mol Cell Res N2 - Many cell stressors block protein translation, inducing formation of cytoplasmic aggregates. These aggregates, named stress granules (SGs), are composed by translationally stalled ribonucleoproteins and their assembly strongly contributes to cell survival. Composition and dynamics of SGs are thus important starting points for identifying critical factors of the stress response. In the present study we link components of the H/ACA snoRNP complexes, highly concentrated in the nucleoli and the Cajal bodies, to SG composition. H/ACA snoRNPs are composed by a core of four highly conserved proteins -dyskerin, Nhp2, Nop10 and Gar1- and are involved in several fundamental processes, including ribosome biogenesis, RNA pseudouridylation, stabilization of small nucleolar RNAs and telomere maintenance. By taking advantage of cells overexpressing a dyskerin splice variant undergoing a dynamic intracellular trafficking, we were able to show that H/ACA snoRNP components can participate in SG formation, this way contributing to the stress response and perhaps transducing signals from the nucleus to the cytoplasm. Collectively, our results show for the first time that H/ACA snoRNP proteins can have additional non-nuclear functions, either independently or interacting with each other, thus further strengthening the close relationship linking nucleolus to SG composition. SN - 1879-2596 UR - https://www.unboundmedicine.com/medline/citation/31412274/A_dynamic_link_between_H/ACA_snoRNP_components_and_cytoplasmic_stress_granules L2 - https://linkinghub.elsevier.com/retrieve/pii/S0167-4889(19)30143-0 DB - PRIME DP - Unbound Medicine ER -