hnRNP F Complexes with Tristetraprolin and Stimulates ARE-mRNA Decay

hnRNP F Complexes with Tristetraprolin and Stimulates ARE-mRNA Decay

The tristetraprolin (TTP) family of zinc-finger proteins, TTP, BRF1 and BRF2, regulate the stability of a subset of mRNAs containing 3′UTR AU-rich elements (AREs), including mRNAs coding for cytokines, transcription factors, and proto-oncogenes. To better understand the mechanism by which TTP-family...

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Main Authors: Reznik, Boris, Clement, Sandra L., Lykke-Andersen, Jens
Format: Online
Language:English
Published: Public Library of Science 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4076271/
id pubmed-4076271
recordtype oai_dc
spelling pubmed-40762712014-07-02 hnRNP F Complexes with Tristetraprolin and Stimulates ARE-mRNA Decay Reznik, Boris Clement, Sandra L. Lykke-Andersen, Jens Research Article The tristetraprolin (TTP) family of zinc-finger proteins, TTP, BRF1 and BRF2, regulate the stability of a subset of mRNAs containing 3′UTR AU-rich elements (AREs), including mRNAs coding for cytokines, transcription factors, and proto-oncogenes. To better understand the mechanism by which TTP-family proteins control mRNA stability in mammalian cells, we aimed to identify TTP- and BRF1-interacting proteins as potential TTP-family co-factors. This revealed hnRNP F as a prominent interactor of TTP and BRF1. While TTP, BRF1 and hnRNP F are all RNA binding proteins (RBPs), the interaction of hnRNP F with TTP and BRF1 is independent of RNA. Depletion of hnRNP F impairs the decay of a subset of TTP-substrate ARE-mRNAs by a mechanism independent of the extent of hnRNP F binding to the mRNA. Taken together, these findings implicate hnRNP F as a co-factor in a subset of TTP/BRF-mediated mRNA decay and highlight the importance of RBP cooperativity in mRNA regulation. Public Library of Science 2014-06-30 /pmc/articles/PMC4076271/ /pubmed/24978456 http://dx.doi.org/10.1371/journal.pone.0100992 Text en © 2014 Reznik et al http://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 properly credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Reznik, Boris
Clement, Sandra L.
Lykke-Andersen, Jens
spellingShingle Reznik, Boris
Clement, Sandra L.
Lykke-Andersen, Jens
hnRNP F Complexes with Tristetraprolin and Stimulates ARE-mRNA Decay
author_facet Reznik, Boris
Clement, Sandra L.
Lykke-Andersen, Jens
author_sort Reznik, Boris
title hnRNP F Complexes with Tristetraprolin and Stimulates ARE-mRNA Decay
title_short hnRNP F Complexes with Tristetraprolin and Stimulates ARE-mRNA Decay
title_full hnRNP F Complexes with Tristetraprolin and Stimulates ARE-mRNA Decay
title_fullStr hnRNP F Complexes with Tristetraprolin and Stimulates ARE-mRNA Decay
title_full_unstemmed hnRNP F Complexes with Tristetraprolin and Stimulates ARE-mRNA Decay
title_sort hnrnp f complexes with tristetraprolin and stimulates are-mrna decay
description The tristetraprolin (TTP) family of zinc-finger proteins, TTP, BRF1 and BRF2, regulate the stability of a subset of mRNAs containing 3′UTR AU-rich elements (AREs), including mRNAs coding for cytokines, transcription factors, and proto-oncogenes. To better understand the mechanism by which TTP-family proteins control mRNA stability in mammalian cells, we aimed to identify TTP- and BRF1-interacting proteins as potential TTP-family co-factors. This revealed hnRNP F as a prominent interactor of TTP and BRF1. While TTP, BRF1 and hnRNP F are all RNA binding proteins (RBPs), the interaction of hnRNP F with TTP and BRF1 is independent of RNA. Depletion of hnRNP F impairs the decay of a subset of TTP-substrate ARE-mRNAs by a mechanism independent of the extent of hnRNP F binding to the mRNA. Taken together, these findings implicate hnRNP F as a co-factor in a subset of TTP/BRF-mediated mRNA decay and highlight the importance of RBP cooperativity in mRNA regulation.
publisher Public Library of Science
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4076271/
_version_ 1612108061738008576

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