Impaired RNA Binding Does Not Prevent Histone Modification Changes in a FUS ALS/FTD Yeast Model

Mutations in the RNA-binding protein FUS are linked to amyotrophic lateral sclerosis and frontotemporal dementia (ALS/FTD). FUS mutants mislocalize and aggregate in dying neurons. We previously established that FUS proteinopathy is linked to changes in the histone modification landscape in a yeast A...

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Autores principales: Bennett, Seth A., Cobos, Samantha N., Son, Elizaveta, Segal, Rianna, Mathew, Shana, Yousuf, Huda, Torrente, Mariana P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Caltech Library 2023
Materias:
New Finding
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10517347/
https://www.ncbi.nlm.nih.gov/pubmed/37746061
http://dx.doi.org/10.17912/micropub.biology.000895
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author Bennett, Seth A.
Cobos, Samantha N.
Son, Elizaveta
Segal, Rianna
Mathew, Shana
Yousuf, Huda
Torrente, Mariana P.
author_facet Bennett, Seth A.
Cobos, Samantha N.
Son, Elizaveta
Segal, Rianna
Mathew, Shana
Yousuf, Huda
Torrente, Mariana P.
author_sort Bennett, Seth A.
collection PubMed
description Mutations in the RNA-binding protein FUS are linked to amyotrophic lateral sclerosis and frontotemporal dementia (ALS/FTD). FUS mutants mislocalize and aggregate in dying neurons. We previously established that FUS proteinopathy is linked to changes in the histone modification landscape in a yeast ALS/FTD model. Here, we examine whether FUS’ RNA binding is necessary for this connection. We find that overexpression of a FUS mutant unable to bind RNA is still associated with reduced levels of H3S10ph, H3K14ac and H3K56ac. Hence, FUS’ ability to bind RNA is not required in the mechanism connecting FUS proteinopathy to altered histone post-translational modifications.
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spelling pubmed-105173472023-09-24 Impaired RNA Binding Does Not Prevent Histone Modification Changes in a FUS ALS/FTD Yeast Model Bennett, Seth A. Cobos, Samantha N. Son, Elizaveta Segal, Rianna Mathew, Shana Yousuf, Huda Torrente, Mariana P. MicroPubl Biol New Finding Mutations in the RNA-binding protein FUS are linked to amyotrophic lateral sclerosis and frontotemporal dementia (ALS/FTD). FUS mutants mislocalize and aggregate in dying neurons. We previously established that FUS proteinopathy is linked to changes in the histone modification landscape in a yeast ALS/FTD model. Here, we examine whether FUS’ RNA binding is necessary for this connection. We find that overexpression of a FUS mutant unable to bind RNA is still associated with reduced levels of H3S10ph, H3K14ac and H3K56ac. Hence, FUS’ ability to bind RNA is not required in the mechanism connecting FUS proteinopathy to altered histone post-translational modifications. Caltech Library 2023-09-08 /pmc/articles/PMC10517347/ /pubmed/37746061 http://dx.doi.org/10.17912/micropub.biology.000895 Text en Copyright: © 2023 by the authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle New Finding
Bennett, Seth A.
Cobos, Samantha N.
Son, Elizaveta
Segal, Rianna
Mathew, Shana
Yousuf, Huda
Torrente, Mariana P.
Impaired RNA Binding Does Not Prevent Histone Modification Changes in a FUS ALS/FTD Yeast Model
title Impaired RNA Binding Does Not Prevent Histone Modification Changes in a FUS ALS/FTD Yeast Model
title_full Impaired RNA Binding Does Not Prevent Histone Modification Changes in a FUS ALS/FTD Yeast Model
title_fullStr Impaired RNA Binding Does Not Prevent Histone Modification Changes in a FUS ALS/FTD Yeast Model
title_full_unstemmed Impaired RNA Binding Does Not Prevent Histone Modification Changes in a FUS ALS/FTD Yeast Model
title_short Impaired RNA Binding Does Not Prevent Histone Modification Changes in a FUS ALS/FTD Yeast Model
title_sort impaired rna binding does not prevent histone modification changes in a fus als/ftd yeast model
topic New Finding
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10517347/
https://www.ncbi.nlm.nih.gov/pubmed/37746061
http://dx.doi.org/10.17912/micropub.biology.000895
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