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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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2020
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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. |
format | Online Article Text |
id | pubmed-7137213 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
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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