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Translation factor and RNA binding protein mRNA interactomes support broader RNA regulons for posttranscriptional control

The regulation of translation provides a rapid and direct mechanism to modulate the cellular proteome. In eukaryotes, an established model for the recruitment of ribosomes to mRNA depends upon a set of conserved translation initiation factors. Nevertheless, how cells orchestrate and define the selec...

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Autores principales: Kershaw, Christopher J., Nelson, Michael G., Castelli, Lydia M., Jennings, Martin D., Lui, Jennifer, Talavera, David, Grant, Chris M., Pavitt, Graham D., Hubbard, Simon J., Ashe, Mark P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10562868/
https://www.ncbi.nlm.nih.gov/pubmed/37633333
http://dx.doi.org/10.1016/j.jbc.2023.105195
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author Kershaw, Christopher J.
Nelson, Michael G.
Castelli, Lydia M.
Jennings, Martin D.
Lui, Jennifer
Talavera, David
Grant, Chris M.
Pavitt, Graham D.
Hubbard, Simon J.
Ashe, Mark P.
author_facet Kershaw, Christopher J.
Nelson, Michael G.
Castelli, Lydia M.
Jennings, Martin D.
Lui, Jennifer
Talavera, David
Grant, Chris M.
Pavitt, Graham D.
Hubbard, Simon J.
Ashe, Mark P.
author_sort Kershaw, Christopher J.
collection PubMed
description The regulation of translation provides a rapid and direct mechanism to modulate the cellular proteome. In eukaryotes, an established model for the recruitment of ribosomes to mRNA depends upon a set of conserved translation initiation factors. Nevertheless, how cells orchestrate and define the selection of individual mRNAs for translation, as opposed to other potential cytosolic fates, is poorly understood. We have previously found significant variation in the interaction between individual mRNAs and an array of translation initiation factors. Indeed, mRNAs can be separated into different classes based upon these interactions to provide a framework for understanding different modes of translation initiation. Here, we extend this approach to include new mRNA interaction profiles for additional proteins involved in shaping the cytoplasmic fate of mRNAs. This work defines a set of seven mRNA clusters, based on their interaction profiles with 12 factors involved in translation and/or RNA binding. The mRNA clusters share both physical and functional characteristics to provide a rationale for the interaction profiles. Moreover, a comparison with mRNA interaction profiles from a host of RNA binding proteins suggests that there are defined patterns in the interactions of functionally related mRNAs. Therefore, this work defines global cytoplasmic mRNA binding modules that likely coordinate the synthesis of functionally related proteins.
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spelling pubmed-105628682023-10-11 Translation factor and RNA binding protein mRNA interactomes support broader RNA regulons for posttranscriptional control Kershaw, Christopher J. Nelson, Michael G. Castelli, Lydia M. Jennings, Martin D. Lui, Jennifer Talavera, David Grant, Chris M. Pavitt, Graham D. Hubbard, Simon J. Ashe, Mark P. J Biol Chem Research Article The regulation of translation provides a rapid and direct mechanism to modulate the cellular proteome. In eukaryotes, an established model for the recruitment of ribosomes to mRNA depends upon a set of conserved translation initiation factors. Nevertheless, how cells orchestrate and define the selection of individual mRNAs for translation, as opposed to other potential cytosolic fates, is poorly understood. We have previously found significant variation in the interaction between individual mRNAs and an array of translation initiation factors. Indeed, mRNAs can be separated into different classes based upon these interactions to provide a framework for understanding different modes of translation initiation. Here, we extend this approach to include new mRNA interaction profiles for additional proteins involved in shaping the cytoplasmic fate of mRNAs. This work defines a set of seven mRNA clusters, based on their interaction profiles with 12 factors involved in translation and/or RNA binding. The mRNA clusters share both physical and functional characteristics to provide a rationale for the interaction profiles. Moreover, a comparison with mRNA interaction profiles from a host of RNA binding proteins suggests that there are defined patterns in the interactions of functionally related mRNAs. Therefore, this work defines global cytoplasmic mRNA binding modules that likely coordinate the synthesis of functionally related proteins. American Society for Biochemistry and Molecular Biology 2023-08-24 /pmc/articles/PMC10562868/ /pubmed/37633333 http://dx.doi.org/10.1016/j.jbc.2023.105195 Text en © 2023 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Research Article
Kershaw, Christopher J.
Nelson, Michael G.
Castelli, Lydia M.
Jennings, Martin D.
Lui, Jennifer
Talavera, David
Grant, Chris M.
Pavitt, Graham D.
Hubbard, Simon J.
Ashe, Mark P.
Translation factor and RNA binding protein mRNA interactomes support broader RNA regulons for posttranscriptional control
title Translation factor and RNA binding protein mRNA interactomes support broader RNA regulons for posttranscriptional control
title_full Translation factor and RNA binding protein mRNA interactomes support broader RNA regulons for posttranscriptional control
title_fullStr Translation factor and RNA binding protein mRNA interactomes support broader RNA regulons for posttranscriptional control
title_full_unstemmed Translation factor and RNA binding protein mRNA interactomes support broader RNA regulons for posttranscriptional control
title_short Translation factor and RNA binding protein mRNA interactomes support broader RNA regulons for posttranscriptional control
title_sort translation factor and rna binding protein mrna interactomes support broader rna regulons for posttranscriptional control
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10562868/
https://www.ncbi.nlm.nih.gov/pubmed/37633333
http://dx.doi.org/10.1016/j.jbc.2023.105195
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