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Polycystic Kidney Disease Ryanodine Receptor Domain (PKDRR) Proteins in Oomycetes
In eukaryotes, two sources of Ca(2+) are accessed to allow rapid changes in the cytosolic levels of this second messenger: the extracellular medium and intracellular Ca(2+) stores, such as the endoplasmic reticulum. One class of channel that permits Ca(2+) entry is the transient receptor potential (...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7399828/ https://www.ncbi.nlm.nih.gov/pubmed/32708691 http://dx.doi.org/10.3390/pathogens9070577 |
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author | Zheng, Limian Prestwich, Barbara Doyle Harrison, Patrick T. Mackrill, John J. |
author_facet | Zheng, Limian Prestwich, Barbara Doyle Harrison, Patrick T. Mackrill, John J. |
author_sort | Zheng, Limian |
collection | PubMed |
description | In eukaryotes, two sources of Ca(2+) are accessed to allow rapid changes in the cytosolic levels of this second messenger: the extracellular medium and intracellular Ca(2+) stores, such as the endoplasmic reticulum. One class of channel that permits Ca(2+) entry is the transient receptor potential (TRP) superfamily, including the polycystic kidney disease (PKD) proteins, or polycystins. Channels that release Ca(2+) from intracellular stores include the inositol 1,4,5-trisphosphate/ryanodine receptor (ITPR/RyR) superfamily. Here, we characterise a family of proteins that are only encoded by oomycete genomes, that we have named PKDRR, since they share domains with both PKD and RyR channels. We provide evidence that these proteins belong to the TRP superfamily and are distinct from the ITPR/RyR superfamily in terms of their evolutionary relationships, protein domain architectures and predicted ion channel structures. We also demonstrate that a hypothetical PKDRR protein from Phytophthora infestans is produced by this organism, is located in the cell-surface membrane and forms multimeric protein complexes. Efforts to functionally characterise this protein in a heterologous expression system were unsuccessful but support a cell-surface localisation. These PKDRR proteins represent potential targets for the development of new “fungicides”, since they are of a distinctive structure that is only found in oomycetes and not in any other cellular organisms. |
format | Online Article Text |
id | pubmed-7399828 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-73998282020-08-17 Polycystic Kidney Disease Ryanodine Receptor Domain (PKDRR) Proteins in Oomycetes Zheng, Limian Prestwich, Barbara Doyle Harrison, Patrick T. Mackrill, John J. Pathogens Article In eukaryotes, two sources of Ca(2+) are accessed to allow rapid changes in the cytosolic levels of this second messenger: the extracellular medium and intracellular Ca(2+) stores, such as the endoplasmic reticulum. One class of channel that permits Ca(2+) entry is the transient receptor potential (TRP) superfamily, including the polycystic kidney disease (PKD) proteins, or polycystins. Channels that release Ca(2+) from intracellular stores include the inositol 1,4,5-trisphosphate/ryanodine receptor (ITPR/RyR) superfamily. Here, we characterise a family of proteins that are only encoded by oomycete genomes, that we have named PKDRR, since they share domains with both PKD and RyR channels. We provide evidence that these proteins belong to the TRP superfamily and are distinct from the ITPR/RyR superfamily in terms of their evolutionary relationships, protein domain architectures and predicted ion channel structures. We also demonstrate that a hypothetical PKDRR protein from Phytophthora infestans is produced by this organism, is located in the cell-surface membrane and forms multimeric protein complexes. Efforts to functionally characterise this protein in a heterologous expression system were unsuccessful but support a cell-surface localisation. These PKDRR proteins represent potential targets for the development of new “fungicides”, since they are of a distinctive structure that is only found in oomycetes and not in any other cellular organisms. MDPI 2020-07-16 /pmc/articles/PMC7399828/ /pubmed/32708691 http://dx.doi.org/10.3390/pathogens9070577 Text en © 2020 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Zheng, Limian Prestwich, Barbara Doyle Harrison, Patrick T. Mackrill, John J. Polycystic Kidney Disease Ryanodine Receptor Domain (PKDRR) Proteins in Oomycetes |
title | Polycystic Kidney Disease Ryanodine Receptor Domain (PKDRR) Proteins in Oomycetes |
title_full | Polycystic Kidney Disease Ryanodine Receptor Domain (PKDRR) Proteins in Oomycetes |
title_fullStr | Polycystic Kidney Disease Ryanodine Receptor Domain (PKDRR) Proteins in Oomycetes |
title_full_unstemmed | Polycystic Kidney Disease Ryanodine Receptor Domain (PKDRR) Proteins in Oomycetes |
title_short | Polycystic Kidney Disease Ryanodine Receptor Domain (PKDRR) Proteins in Oomycetes |
title_sort | polycystic kidney disease ryanodine receptor domain (pkdrr) proteins in oomycetes |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7399828/ https://www.ncbi.nlm.nih.gov/pubmed/32708691 http://dx.doi.org/10.3390/pathogens9070577 |
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