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DDX20: A Multifunctional Complex Protein

DEAD-box decapping enzyme 20 (DDX20) is a putative RNA-decapping enzyme that can be identified by the conserved motif Asp–Glu–Ala–Asp (DEAD). Cellular processes involve numerous RNA secondary structure alterations, including translation initiation, nuclear and mitochondrial splicing, and assembly of...

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Autores principales: He, Lu, Yang, Jinke, Hao, Yu, Yang, Xing, Shi, Xijuan, Zhang, Dajun, Zhao, Dengshuai, Yan, Wenqian, Bie, Xintian, Chen, Lingling, Chen, Guohui, Zhao, Siyue, Liu, Xiangtao, Zheng, Haixue, Zhang, Keshan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10608988/
https://www.ncbi.nlm.nih.gov/pubmed/37894677
http://dx.doi.org/10.3390/molecules28207198
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author He, Lu
Yang, Jinke
Hao, Yu
Yang, Xing
Shi, Xijuan
Zhang, Dajun
Zhao, Dengshuai
Yan, Wenqian
Bie, Xintian
Chen, Lingling
Chen, Guohui
Zhao, Siyue
Liu, Xiangtao
Zheng, Haixue
Zhang, Keshan
author_facet He, Lu
Yang, Jinke
Hao, Yu
Yang, Xing
Shi, Xijuan
Zhang, Dajun
Zhao, Dengshuai
Yan, Wenqian
Bie, Xintian
Chen, Lingling
Chen, Guohui
Zhao, Siyue
Liu, Xiangtao
Zheng, Haixue
Zhang, Keshan
author_sort He, Lu
collection PubMed
description DEAD-box decapping enzyme 20 (DDX20) is a putative RNA-decapping enzyme that can be identified by the conserved motif Asp–Glu–Ala–Asp (DEAD). Cellular processes involve numerous RNA secondary structure alterations, including translation initiation, nuclear and mitochondrial splicing, and assembly of ribosomes and spliceosomes. DDX20 reportedly plays an important role in cellular transcription and post-transcriptional modifications. On the one hand, DDX20 can interact with various transcription factors and repress the transcriptional process. On the other hand, DDX20 forms the survival motor neuron complex and participates in the assembly of snRNP, ultimately affecting the RNA splicing process. Finally, DDX20 can potentially rely on its RNA-unwinding enzyme function to participate in microRNA (miRNA) maturation and act as a component of the RNA-induced silencing complex. In addition, although DDX20 is not a key component in the innate immune system signaling pathway, it can affect the nuclear factor kappa B (NF-κB) and p53 signaling pathways. In particular, DDX20 plays different roles in tumorigenesis development through the NF-κB signaling pathway. This process is regulated by various factors such as miRNA. DDX20 can influence processes such as viral replication in cells by interacting with two proteins in Epstein–Barr virus and can regulate the replication process of several viruses through the innate immune system, indicating that DDX20 plays an important role in the innate immune system. Herein, we review the effects of DDX20 on the innate immune system and its role in transcriptional and post-transcriptional modification processes, based on which we provide an outlook on the future of DDX20 research in innate immunity and viral infections.
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spelling pubmed-106089882023-10-28 DDX20: A Multifunctional Complex Protein He, Lu Yang, Jinke Hao, Yu Yang, Xing Shi, Xijuan Zhang, Dajun Zhao, Dengshuai Yan, Wenqian Bie, Xintian Chen, Lingling Chen, Guohui Zhao, Siyue Liu, Xiangtao Zheng, Haixue Zhang, Keshan Molecules Review DEAD-box decapping enzyme 20 (DDX20) is a putative RNA-decapping enzyme that can be identified by the conserved motif Asp–Glu–Ala–Asp (DEAD). Cellular processes involve numerous RNA secondary structure alterations, including translation initiation, nuclear and mitochondrial splicing, and assembly of ribosomes and spliceosomes. DDX20 reportedly plays an important role in cellular transcription and post-transcriptional modifications. On the one hand, DDX20 can interact with various transcription factors and repress the transcriptional process. On the other hand, DDX20 forms the survival motor neuron complex and participates in the assembly of snRNP, ultimately affecting the RNA splicing process. Finally, DDX20 can potentially rely on its RNA-unwinding enzyme function to participate in microRNA (miRNA) maturation and act as a component of the RNA-induced silencing complex. In addition, although DDX20 is not a key component in the innate immune system signaling pathway, it can affect the nuclear factor kappa B (NF-κB) and p53 signaling pathways. In particular, DDX20 plays different roles in tumorigenesis development through the NF-κB signaling pathway. This process is regulated by various factors such as miRNA. DDX20 can influence processes such as viral replication in cells by interacting with two proteins in Epstein–Barr virus and can regulate the replication process of several viruses through the innate immune system, indicating that DDX20 plays an important role in the innate immune system. Herein, we review the effects of DDX20 on the innate immune system and its role in transcriptional and post-transcriptional modification processes, based on which we provide an outlook on the future of DDX20 research in innate immunity and viral infections. MDPI 2023-10-20 /pmc/articles/PMC10608988/ /pubmed/37894677 http://dx.doi.org/10.3390/molecules28207198 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
He, Lu
Yang, Jinke
Hao, Yu
Yang, Xing
Shi, Xijuan
Zhang, Dajun
Zhao, Dengshuai
Yan, Wenqian
Bie, Xintian
Chen, Lingling
Chen, Guohui
Zhao, Siyue
Liu, Xiangtao
Zheng, Haixue
Zhang, Keshan
DDX20: A Multifunctional Complex Protein
title DDX20: A Multifunctional Complex Protein
title_full DDX20: A Multifunctional Complex Protein
title_fullStr DDX20: A Multifunctional Complex Protein
title_full_unstemmed DDX20: A Multifunctional Complex Protein
title_short DDX20: A Multifunctional Complex Protein
title_sort ddx20: a multifunctional complex protein
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10608988/
https://www.ncbi.nlm.nih.gov/pubmed/37894677
http://dx.doi.org/10.3390/molecules28207198
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