Cargando…

An atlas of posttranslational modifications on RNA binding proteins

RNA structure and function are intimately tied to RNA binding protein recognition and regulation. Posttranslational modifications are chemical modifications which can control protein biology. The role of PTMs in the regulation RBPs is not well understood, in part due to a lacking analysis of PTM dep...

Descripción completa

Detalles Bibliográficos
Autores principales: England, Whitney E, Wang, Jingtian, Chen, Siwei, Baldi, Pierre, Flynn, Ryan A, Spitale, Robert C
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9071496/
https://www.ncbi.nlm.nih.gov/pubmed/35438783
http://dx.doi.org/10.1093/nar/gkac243
_version_ 1784700853982068736
author England, Whitney E
Wang, Jingtian
Chen, Siwei
Baldi, Pierre
Flynn, Ryan A
Spitale, Robert C
author_facet England, Whitney E
Wang, Jingtian
Chen, Siwei
Baldi, Pierre
Flynn, Ryan A
Spitale, Robert C
author_sort England, Whitney E
collection PubMed
description RNA structure and function are intimately tied to RNA binding protein recognition and regulation. Posttranslational modifications are chemical modifications which can control protein biology. The role of PTMs in the regulation RBPs is not well understood, in part due to a lacking analysis of PTM deposition on RBPs. Herein, we present an analysis of posttranslational modifications (PTMs) on RNA binding proteins (RBPs; a PTM RBP Atlas). We curate published datasets and primary literature to understand the landscape of PTMs and use protein–protein interaction data to understand and potentially provide a framework for understanding which enzymes are controlling PTM deposition and removal on the RBP landscape. Intersection of our data with The Cancer Genome Atlas also provides researchers understanding of mutations that would alter PTM deposition. Additional characterization of the RNA–protein interface provided from in-cell UV crosslinking experiments provides a framework for hypotheses about which PTMs could be regulating RNA binding and thus RBP function. Finally, we provide an online database for our data that is easy to use for the community. It is our hope our efforts will provide researchers will an invaluable tool to test the function of PTMs controlling RBP function and thus RNA biology.
format Online
Article
Text
id pubmed-9071496
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Oxford University Press
record_format MEDLINE/PubMed
spelling pubmed-90714962022-05-06 An atlas of posttranslational modifications on RNA binding proteins England, Whitney E Wang, Jingtian Chen, Siwei Baldi, Pierre Flynn, Ryan A Spitale, Robert C Nucleic Acids Res Data Resources and Analyses RNA structure and function are intimately tied to RNA binding protein recognition and regulation. Posttranslational modifications are chemical modifications which can control protein biology. The role of PTMs in the regulation RBPs is not well understood, in part due to a lacking analysis of PTM deposition on RBPs. Herein, we present an analysis of posttranslational modifications (PTMs) on RNA binding proteins (RBPs; a PTM RBP Atlas). We curate published datasets and primary literature to understand the landscape of PTMs and use protein–protein interaction data to understand and potentially provide a framework for understanding which enzymes are controlling PTM deposition and removal on the RBP landscape. Intersection of our data with The Cancer Genome Atlas also provides researchers understanding of mutations that would alter PTM deposition. Additional characterization of the RNA–protein interface provided from in-cell UV crosslinking experiments provides a framework for hypotheses about which PTMs could be regulating RNA binding and thus RBP function. Finally, we provide an online database for our data that is easy to use for the community. It is our hope our efforts will provide researchers will an invaluable tool to test the function of PTMs controlling RBP function and thus RNA biology. Oxford University Press 2022-04-19 /pmc/articles/PMC9071496/ /pubmed/35438783 http://dx.doi.org/10.1093/nar/gkac243 Text en © The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Data Resources and Analyses
England, Whitney E
Wang, Jingtian
Chen, Siwei
Baldi, Pierre
Flynn, Ryan A
Spitale, Robert C
An atlas of posttranslational modifications on RNA binding proteins
title An atlas of posttranslational modifications on RNA binding proteins
title_full An atlas of posttranslational modifications on RNA binding proteins
title_fullStr An atlas of posttranslational modifications on RNA binding proteins
title_full_unstemmed An atlas of posttranslational modifications on RNA binding proteins
title_short An atlas of posttranslational modifications on RNA binding proteins
title_sort atlas of posttranslational modifications on rna binding proteins
topic Data Resources and Analyses
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9071496/
https://www.ncbi.nlm.nih.gov/pubmed/35438783
http://dx.doi.org/10.1093/nar/gkac243
work_keys_str_mv AT englandwhitneye anatlasofposttranslationalmodificationsonrnabindingproteins
AT wangjingtian anatlasofposttranslationalmodificationsonrnabindingproteins
AT chensiwei anatlasofposttranslationalmodificationsonrnabindingproteins
AT baldipierre anatlasofposttranslationalmodificationsonrnabindingproteins
AT flynnryana anatlasofposttranslationalmodificationsonrnabindingproteins
AT spitalerobertc anatlasofposttranslationalmodificationsonrnabindingproteins
AT englandwhitneye atlasofposttranslationalmodificationsonrnabindingproteins
AT wangjingtian atlasofposttranslationalmodificationsonrnabindingproteins
AT chensiwei atlasofposttranslationalmodificationsonrnabindingproteins
AT baldipierre atlasofposttranslationalmodificationsonrnabindingproteins
AT flynnryana atlasofposttranslationalmodificationsonrnabindingproteins
AT spitalerobertc atlasofposttranslationalmodificationsonrnabindingproteins