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Comparative and evolutionary analysis of RIP kinases in immune responses

The group of receptor-interacting protein (RIP) kinases has seven members (RIPK1–7), with one homologous kinase domain but distinct non-kinase regions. Although RIPK1–3 have emerged as key modulators of inflammation and cell death, few studies have connected RIPK4–7 to immune responses. The divergen...

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Autores principales: Lv, Shangge, Jiang, Yu, Li, Yuzheng, Huang, Ruilin, Peng, Lingyu, Ma, Zhaoyin, Lu, Nan, Lin, Xiaoying, Yan, Jie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9573974/
https://www.ncbi.nlm.nih.gov/pubmed/36263437
http://dx.doi.org/10.3389/fgene.2022.796291
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author Lv, Shangge
Jiang, Yu
Li, Yuzheng
Huang, Ruilin
Peng, Lingyu
Ma, Zhaoyin
Lu, Nan
Lin, Xiaoying
Yan, Jie
author_facet Lv, Shangge
Jiang, Yu
Li, Yuzheng
Huang, Ruilin
Peng, Lingyu
Ma, Zhaoyin
Lu, Nan
Lin, Xiaoying
Yan, Jie
author_sort Lv, Shangge
collection PubMed
description The group of receptor-interacting protein (RIP) kinases has seven members (RIPK1–7), with one homologous kinase domain but distinct non-kinase regions. Although RIPK1–3 have emerged as key modulators of inflammation and cell death, few studies have connected RIPK4–7 to immune responses. The divergence in domain structures and paralogue information in the Ensembl database have raised question about the phylogeny of RIPK1–7. In this study, phylogenetic trees of RIPK1–7 and paralogues constructed using full-length amino acid sequences or Kinase domain demonstrate that RIPK6 and RIPK7 are distinct from RIPK1–5 and paralogues shown in the Ensembl database are inaccurate. Comparative and evolutionary analyses were subsequently performed to gain new clues about the potential functions of RIPK3–7. RIPK3 gene loss in birds and animals that undergo torpor, a common physiological phenomenon in cold environments, implies that RIPK3 may be involved in ischemia-reperfusion injury and/or high metabolic rate. The negligible expression of RIPK4 and RIPK5 in immune cells is likely responsible for the lack of studies on the direct role of these members in immunity; RIPK6 and RIPK7 are conserved among plants, invertebrates and vertebrates, and dominantly expressed in innate immune cells, indicating their roles in innate immunity. Overall, our results provide insights into the multifaceted and conserved biochemical functions of RIP kinases.
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spelling pubmed-95739742022-10-18 Comparative and evolutionary analysis of RIP kinases in immune responses Lv, Shangge Jiang, Yu Li, Yuzheng Huang, Ruilin Peng, Lingyu Ma, Zhaoyin Lu, Nan Lin, Xiaoying Yan, Jie Front Genet Genetics The group of receptor-interacting protein (RIP) kinases has seven members (RIPK1–7), with one homologous kinase domain but distinct non-kinase regions. Although RIPK1–3 have emerged as key modulators of inflammation and cell death, few studies have connected RIPK4–7 to immune responses. The divergence in domain structures and paralogue information in the Ensembl database have raised question about the phylogeny of RIPK1–7. In this study, phylogenetic trees of RIPK1–7 and paralogues constructed using full-length amino acid sequences or Kinase domain demonstrate that RIPK6 and RIPK7 are distinct from RIPK1–5 and paralogues shown in the Ensembl database are inaccurate. Comparative and evolutionary analyses were subsequently performed to gain new clues about the potential functions of RIPK3–7. RIPK3 gene loss in birds and animals that undergo torpor, a common physiological phenomenon in cold environments, implies that RIPK3 may be involved in ischemia-reperfusion injury and/or high metabolic rate. The negligible expression of RIPK4 and RIPK5 in immune cells is likely responsible for the lack of studies on the direct role of these members in immunity; RIPK6 and RIPK7 are conserved among plants, invertebrates and vertebrates, and dominantly expressed in innate immune cells, indicating their roles in innate immunity. Overall, our results provide insights into the multifaceted and conserved biochemical functions of RIP kinases. Frontiers Media S.A. 2022-10-03 /pmc/articles/PMC9573974/ /pubmed/36263437 http://dx.doi.org/10.3389/fgene.2022.796291 Text en Copyright © 2022 Lv, Jiang, Li, Huang, Peng, Ma, Lu, Lin and Yan. https://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 Genetics
Lv, Shangge
Jiang, Yu
Li, Yuzheng
Huang, Ruilin
Peng, Lingyu
Ma, Zhaoyin
Lu, Nan
Lin, Xiaoying
Yan, Jie
Comparative and evolutionary analysis of RIP kinases in immune responses
title Comparative and evolutionary analysis of RIP kinases in immune responses
title_full Comparative and evolutionary analysis of RIP kinases in immune responses
title_fullStr Comparative and evolutionary analysis of RIP kinases in immune responses
title_full_unstemmed Comparative and evolutionary analysis of RIP kinases in immune responses
title_short Comparative and evolutionary analysis of RIP kinases in immune responses
title_sort comparative and evolutionary analysis of rip kinases in immune responses
topic Genetics
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9573974/
https://www.ncbi.nlm.nih.gov/pubmed/36263437
http://dx.doi.org/10.3389/fgene.2022.796291
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