A novel function of human Pumilio proteins in cytoplasmic sensing of viral infection.
RIG-I-like receptor (RLR) plays a pivotal role in the detection of invading pathogens to initiate type I interferon (IFN) gene transcription. Since aberrant IFN production is harmful, RLR signaling is strictly regulated. However, the regulatory mechanisms are not fully understood. By expression clon...
Main Authors: | , , , , , , , |
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Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2014-10-01
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Series: | PLoS Pathogens |
Online Access: | http://europepmc.org/articles/PMC4207803?pdf=render |
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author | Ryo Narita Kiyohiro Takahasi Etsu Murakami Emi Hirano Seiji P Yamamoto Mitsutoshi Yoneyama Hiroki Kato Takashi Fujita |
author_facet | Ryo Narita Kiyohiro Takahasi Etsu Murakami Emi Hirano Seiji P Yamamoto Mitsutoshi Yoneyama Hiroki Kato Takashi Fujita |
author_sort | Ryo Narita |
collection | DOAJ |
description | RIG-I-like receptor (RLR) plays a pivotal role in the detection of invading pathogens to initiate type I interferon (IFN) gene transcription. Since aberrant IFN production is harmful, RLR signaling is strictly regulated. However, the regulatory mechanisms are not fully understood. By expression cloning, we identified Pumilio proteins, PUM1 and PUM2, as candidate positive regulators of RIG-I signaling. Overexpression of Pumilio proteins and their knockdown augmented and diminished IFN-β promoter activity induced by Newcastle disease virus (NDV), respectively. Both proteins showed a specific association with LGP2, but not with RIG-I or MDA5. Furthermore, all of these components were recruited to NDV-induced antiviral stress granules. Interestingly, biochemical analyses revealed that Pumilio increased double-stranded (ds) RNA binding affinity of LGP2; however, Pumilio was absent in the dsRNA-LGP2 complex, suggesting that Pumilio facilitates viral RNA recognition by LGP2 through its chaperon-like function. Collectively, our results demonstrate an unknown function of Pumilio in viral recognition by LGP2. |
first_indexed | 2024-04-12T07:04:51Z |
format | Article |
id | doaj.art-6d58c480e109408b8f3a596e4b84af2b |
institution | Directory Open Access Journal |
issn | 1553-7366 1553-7374 |
language | English |
last_indexed | 2024-04-12T07:04:51Z |
publishDate | 2014-10-01 |
publisher | Public Library of Science (PLoS) |
record_format | Article |
series | PLoS Pathogens |
spelling | doaj.art-6d58c480e109408b8f3a596e4b84af2b2022-12-22T03:42:50ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742014-10-011010e100441710.1371/journal.ppat.1004417A novel function of human Pumilio proteins in cytoplasmic sensing of viral infection.Ryo NaritaKiyohiro TakahasiEtsu MurakamiEmi HiranoSeiji P YamamotoMitsutoshi YoneyamaHiroki KatoTakashi FujitaRIG-I-like receptor (RLR) plays a pivotal role in the detection of invading pathogens to initiate type I interferon (IFN) gene transcription. Since aberrant IFN production is harmful, RLR signaling is strictly regulated. However, the regulatory mechanisms are not fully understood. By expression cloning, we identified Pumilio proteins, PUM1 and PUM2, as candidate positive regulators of RIG-I signaling. Overexpression of Pumilio proteins and their knockdown augmented and diminished IFN-β promoter activity induced by Newcastle disease virus (NDV), respectively. Both proteins showed a specific association with LGP2, but not with RIG-I or MDA5. Furthermore, all of these components were recruited to NDV-induced antiviral stress granules. Interestingly, biochemical analyses revealed that Pumilio increased double-stranded (ds) RNA binding affinity of LGP2; however, Pumilio was absent in the dsRNA-LGP2 complex, suggesting that Pumilio facilitates viral RNA recognition by LGP2 through its chaperon-like function. Collectively, our results demonstrate an unknown function of Pumilio in viral recognition by LGP2.http://europepmc.org/articles/PMC4207803?pdf=render |
spellingShingle | Ryo Narita Kiyohiro Takahasi Etsu Murakami Emi Hirano Seiji P Yamamoto Mitsutoshi Yoneyama Hiroki Kato Takashi Fujita A novel function of human Pumilio proteins in cytoplasmic sensing of viral infection. PLoS Pathogens |
title | A novel function of human Pumilio proteins in cytoplasmic sensing of viral infection. |
title_full | A novel function of human Pumilio proteins in cytoplasmic sensing of viral infection. |
title_fullStr | A novel function of human Pumilio proteins in cytoplasmic sensing of viral infection. |
title_full_unstemmed | A novel function of human Pumilio proteins in cytoplasmic sensing of viral infection. |
title_short | A novel function of human Pumilio proteins in cytoplasmic sensing of viral infection. |
title_sort | novel function of human pumilio proteins in cytoplasmic sensing of viral infection |
url | http://europepmc.org/articles/PMC4207803?pdf=render |
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