ELAVL1 primarily couples mRNA stability with the 3' UTRs of interferon-stimulated genes.


Journal

Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691

Informations de publication

Date de publication:
25 05 2021
Historique:
received: 17 09 2020
revised: 13 03 2021
accepted: 04 05 2021
entrez: 26 5 2021
pubmed: 27 5 2021
medline: 11 2 2022
Statut: ppublish

Résumé

Upon pathogen detection, the innate immune system triggers signaling events leading to upregulation of pro-inflammatory and anti-microbial mRNA transcripts. RNA-binding proteins (RBPs) interact with these critical mRNAs and regulate their fates at the post-transcriptional level. One such RBP is ELAVL1. Although significant progress has been made in understanding how embryonic lethal vision-like protein 1 (ELAVL1) regulates mRNAs, its target repertoire and binding distribution within an immunological context remain poorly understood. We overlap four high-throughput approaches to define its context-dependent targets and determine its regulatory impact during immune activation. ELAVL1 transitions from binding overwhelmingly intronic sites to 3' UTR sites upon immune stimulation of cells, binding previously and newly expressed mRNAs. We find that ELAVL1 mediates the RNA stability of genes that regulate pathways essential to pathogen sensing and cytokine production. Our findings reveal the importance of examining RBP regulatory impact under dynamic transcriptomic events to understand their post-transcriptional regulatory roles within specific biological circuitries.

Identifiants

pubmed: 34038724
pii: S2211-1247(21)00523-4
doi: 10.1016/j.celrep.2021.109178
pmc: PMC8225249
mid: NIHMS1708606
pii:
doi:

Substances chimiques

3' Untranslated Regions 0
ELAV-Like Protein 1 0
RNA, Messenger 0
Interferons 9008-11-1

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

109178

Subventions

Organisme : NIGMS NIH HHS
ID : R35 GM119569
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM065086
Pays : United States
Organisme : NCATS NIH HHS
ID : UL1 TR002243
Pays : United States

Informations de copyright

Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

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Auteurs

Katherine Rothamel (K)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.

Sarah Arcos (S)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.

Byungil Kim (B)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.

Clara Reasoner (C)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.

Samantha Lisy (S)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.

Neelanjan Mukherjee (N)

Department of Biochemistry and Molecular Genetics, University of Colorado School of Medicine, Aurora, CO 80045, USA.

Manuel Ascano (M)

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. Electronic address: manuel.ascano@vanderbilt.edu.

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Classifications MeSH