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-f...

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Main Authors: Boris Reznik, Sandra L Clement, Jens Lykke-Andersen
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4076271?pdf=render
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author Boris Reznik
Sandra L Clement
Jens Lykke-Andersen
author_facet Boris Reznik
Sandra L Clement
Jens Lykke-Andersen
author_sort Boris Reznik
collection DOAJ
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.
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spelling doaj.art-fdba22b08aad43da81f84c85a755302e2022-12-22T03:36:11ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0196e10099210.1371/journal.pone.0100992hnRNP F complexes with tristetraprolin and stimulates ARE-mRNA decay.Boris ReznikSandra L ClementJens Lykke-AndersenThe 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.http://europepmc.org/articles/PMC4076271?pdf=render
spellingShingle Boris Reznik
Sandra L Clement
Jens Lykke-Andersen
hnRNP F complexes with tristetraprolin and stimulates ARE-mRNA decay.
PLoS ONE
title 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_short hnRNP F complexes with tristetraprolin and stimulates ARE-mRNA decay.
title_sort hnrnp f complexes with tristetraprolin and stimulates are mrna decay
url http://europepmc.org/articles/PMC4076271?pdf=render
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