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PKZ, a Fish-Unique eIF2α Kinase Involved in Innate Immune Response

PKZ is a novel and unique eIF2α protein kinase identified in fish. Although PKZ is most homologous to PKR, particularly in the C-terminal catalytic domain, it contains two N-terminal Z-DNA-binding domains (Zα1 and Zα2) instead of the dsRNA binding domains (dsRBDs) in PKR. As a novel member of eIF2α...

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Detalles Bibliográficos
Autores principales: Wu, Chuxin, Zhang, Yibing, Hu, Chengyu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7137213/
https://www.ncbi.nlm.nih.gov/pubmed/32296447
http://dx.doi.org/10.3389/fimmu.2020.00585
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author Wu, Chuxin
Zhang, Yibing
Hu, Chengyu
author_facet Wu, Chuxin
Zhang, Yibing
Hu, Chengyu
author_sort Wu, Chuxin
collection PubMed
description PKZ is a novel and unique eIF2α protein kinase identified in fish. Although PKZ is most homologous to PKR, particularly in the C-terminal catalytic domain, it contains two N-terminal Z-DNA-binding domains (Zα1 and Zα2) instead of the dsRNA binding domains (dsRBDs) in PKR. As a novel member of eIF2α kinase family, the available data suggest that PKZ has some distinct mechanisms for recognition, binding, and B-Z DNA transition. Functionally, PKZ seems to be activated by the binding of Zα to Z-DNA and participates in innate immune responses. In this review, we summarize the recent progress on fish PKZ.
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spelling pubmed-71372132020-04-15 PKZ, a Fish-Unique eIF2α Kinase Involved in Innate Immune Response Wu, Chuxin Zhang, Yibing Hu, Chengyu Front Immunol Immunology PKZ is a novel and unique eIF2α protein kinase identified in fish. Although PKZ is most homologous to PKR, particularly in the C-terminal catalytic domain, it contains two N-terminal Z-DNA-binding domains (Zα1 and Zα2) instead of the dsRNA binding domains (dsRBDs) in PKR. As a novel member of eIF2α kinase family, the available data suggest that PKZ has some distinct mechanisms for recognition, binding, and B-Z DNA transition. Functionally, PKZ seems to be activated by the binding of Zα to Z-DNA and participates in innate immune responses. In this review, we summarize the recent progress on fish PKZ. Frontiers Media S.A. 2020-03-31 /pmc/articles/PMC7137213/ /pubmed/32296447 http://dx.doi.org/10.3389/fimmu.2020.00585 Text en Copyright © 2020 Wu, Zhang and Hu. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Immunology
Wu, Chuxin
Zhang, Yibing
Hu, Chengyu
PKZ, a Fish-Unique eIF2α Kinase Involved in Innate Immune Response
title PKZ, a Fish-Unique eIF2α Kinase Involved in Innate Immune Response
title_full PKZ, a Fish-Unique eIF2α Kinase Involved in Innate Immune Response
title_fullStr PKZ, a Fish-Unique eIF2α Kinase Involved in Innate Immune Response
title_full_unstemmed PKZ, a Fish-Unique eIF2α Kinase Involved in Innate Immune Response
title_short PKZ, a Fish-Unique eIF2α Kinase Involved in Innate Immune Response
title_sort pkz, a fish-unique eif2α kinase involved in innate immune response
topic Immunology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7137213/
https://www.ncbi.nlm.nih.gov/pubmed/32296447
http://dx.doi.org/10.3389/fimmu.2020.00585
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