Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain
Samsonova et al. show a cooperative association of Lin28 and YB-1 for their target mRNA through their cold-shock domain, which is a conserved β-barrel structure that binds to single-stranded RNA. This study suggests that the association of Lin28 with YB-1 in mRNPs may contribute to the translational...
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2021
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oai:doaj.org-article:15258b4c3a3942419e49124926949c3e2021-12-02T13:17:48ZLin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain10.1038/s42003-021-01862-32399-3642https://doaj.org/article/15258b4c3a3942419e49124926949c3e2021-03-01T00:00:00Zhttps://doi.org/10.1038/s42003-021-01862-3https://doaj.org/toc/2399-3642Samsonova et al. show a cooperative association of Lin28 and YB-1 for their target mRNA through their cold-shock domain, which is a conserved β-barrel structure that binds to single-stranded RNA. This study suggests that the association of Lin28 with YB-1 in mRNPs may contribute to the translational plasticity during development and the adaptation of cancer cells to adverse environments.Anastasiia SamsonovaKrystel El HageBénédicte DesforgesVandana JoshiMarie-Jeanne ClémentGuillaume LambertHélène HenrieNicolas BabaultPierrick CraveurRachid C. MarounEmilie SteinerAhmed BouhssAlexandre MaucuerDmitry N. LyabinLev P. OvchinnikovLoic HamonDavid PastréNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-16 (2021) |
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Biology (General) QH301-705.5 |
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Biology (General) QH301-705.5 Anastasiia Samsonova Krystel El Hage Bénédicte Desforges Vandana Joshi Marie-Jeanne Clément Guillaume Lambert Hélène Henrie Nicolas Babault Pierrick Craveur Rachid C. Maroun Emilie Steiner Ahmed Bouhss Alexandre Maucuer Dmitry N. Lyabin Lev P. Ovchinnikov Loic Hamon David Pastré Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain |
description |
Samsonova et al. show a cooperative association of Lin28 and YB-1 for their target mRNA through their cold-shock domain, which is a conserved β-barrel structure that binds to single-stranded RNA. This study suggests that the association of Lin28 with YB-1 in mRNPs may contribute to the translational plasticity during development and the adaptation of cancer cells to adverse environments. |
format |
article |
author |
Anastasiia Samsonova Krystel El Hage Bénédicte Desforges Vandana Joshi Marie-Jeanne Clément Guillaume Lambert Hélène Henrie Nicolas Babault Pierrick Craveur Rachid C. Maroun Emilie Steiner Ahmed Bouhss Alexandre Maucuer Dmitry N. Lyabin Lev P. Ovchinnikov Loic Hamon David Pastré |
author_facet |
Anastasiia Samsonova Krystel El Hage Bénédicte Desforges Vandana Joshi Marie-Jeanne Clément Guillaume Lambert Hélène Henrie Nicolas Babault Pierrick Craveur Rachid C. Maroun Emilie Steiner Ahmed Bouhss Alexandre Maucuer Dmitry N. Lyabin Lev P. Ovchinnikov Loic Hamon David Pastré |
author_sort |
Anastasiia Samsonova |
title |
Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain |
title_short |
Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain |
title_full |
Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain |
title_fullStr |
Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain |
title_full_unstemmed |
Lin28, a major translation reprogramming factor, gains access to YB-1-packaged mRNA through its cold-shock domain |
title_sort |
lin28, a major translation reprogramming factor, gains access to yb-1-packaged mrna through its cold-shock domain |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/15258b4c3a3942419e49124926949c3e |
work_keys_str_mv |
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