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Plasticity of nuclear and cytoplasmic stress responses of RNA-binding proteins

Cellular stress causes multifaceted reactions to trigger adaptive responses to environmental cues at all levels of the gene expression pathway. RNA-binding proteins (RBP) are key contributors to stress-induced regulation of RNA fate and function. Here, we uncover the plasticity of the RNA interactom...

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Detalles Bibliográficos
Autores principales: Backlund, Michael, Stein, Frank, Rettel, Mandy, Schwarzl, Thomas, Perez-Perri, Joel I, Brosig, Annika, Zhou, Yang, Neu-Yilik, Gabriele, Hentze, Matthias W, Kulozik, Andreas E
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7229827/
https://www.ncbi.nlm.nih.gov/pubmed/32313943
http://dx.doi.org/10.1093/nar/gkaa256
Descripción
Sumario:Cellular stress causes multifaceted reactions to trigger adaptive responses to environmental cues at all levels of the gene expression pathway. RNA-binding proteins (RBP) are key contributors to stress-induced regulation of RNA fate and function. Here, we uncover the plasticity of the RNA interactome in stressed cells, differentiating between responses in the nucleus and in the cytoplasm. We applied enhanced RNA interactome capture (eRIC) analysis preceded by nucleo-cytoplasmic fractionation following arsenite-induced oxidative stress. The data reveal unexpectedly compartmentalized RNA interactomes and their responses to stress, including differential responses of RBPs in the nucleus versus the cytoplasm, which would have been missed by whole cell analyses.