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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Format: | Article |
Language: | English |
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Public Library of Science (PLoS)
2014-01-01
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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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id | doaj.art-fdba22b08aad43da81f84c85a755302e |
institution | Directory Open Access Journal |
issn | 1932-6203 |
language | English |
last_indexed | 2024-04-12T10:52:50Z |
publishDate | 2014-01-01 |
publisher | Public Library of Science (PLoS) |
record_format | Article |
series | PLoS ONE |
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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