Polycystic Kidney Disease Ryanodine Receptor Domain (PKDRR) Proteins in Oomycetes.
Identifieur interne : 000085 ( Main/Exploration ); précédent : 000084; suivant : 000086Polycystic Kidney Disease Ryanodine Receptor Domain (PKDRR) Proteins in Oomycetes.
Auteurs : Limian Zheng [Irlande (pays)] ; Barbara Doyle Prestwich [Irlande (pays)] ; Patrick T. Harrison [Irlande (pays)] ; John J. Mackrill [Irlande (pays)]Source :
- Pathogens (Basel, Switzerland) [ 2076-0817 ] ; 2020.
Abstract
In eukaryotes, two sources of Ca2+ are accessed to allow rapid changes in the cytosolic levels of this second messenger: the extracellular medium and intracellular Ca2+ stores, such as the endoplasmic reticulum. One class of channel that permits Ca2+ entry is the transient receptor potential (TRP) superfamily, including the polycystic kidney disease (PKD) proteins, or polycystins. Channels that release Ca2+ 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.
DOI: 10.3390/pathogens9070577
PubMed: 32708691
PubMed Central: PMC7399828
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Harrison</name><affiliation wicri:level="1"><nlm:affiliation>Department of Physiology, School of Medicine, University College Cork, T12 XF62 Cork, Ireland.</nlm:affiliation><country xml:lang="fr">Irlande (pays)</country><wicri:regionArea>Department of Physiology, School of Medicine, University College Cork, T12 XF62 Cork</wicri:regionArea><wicri:noRegion>T12 XF62 Cork</wicri:noRegion></affiliation></author><author><name sortKey="Mackrill, John J" sort="Mackrill, John J" uniqKey="Mackrill J" first="John J" last="Mackrill">John J. Mackrill</name><affiliation wicri:level="1"><nlm:affiliation>Department of Physiology, School of Medicine, University College Cork, T12 XF62 Cork, Ireland.</nlm:affiliation><country xml:lang="fr">Irlande (pays)</country><wicri:regionArea>Department of Physiology, School of Medicine, University College Cork, T12 XF62 Cork</wicri:regionArea><wicri:noRegion>T12 XF62 Cork</wicri:noRegion></affiliation></author></analytic><series><title level="j">Pathogens (Basel, Switzerland)</title><idno type="ISSN">2076-0817</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In eukaryotes, two sources of Ca<sup>2+</sup> are accessed to allow rapid changes in the cytosolic levels of this second messenger: the extracellular medium and intracellular Ca<sup>2+</sup> stores, such as the endoplasmic reticulum. One class of channel that permits Ca<sup>2+</sup> entry is the transient receptor potential (TRP) superfamily, including the polycystic kidney disease (PKD) proteins, or polycystins. Channels that release Ca<sup>2+</sup> 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 <i>Phytophthora infestans</i> 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.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">32708691</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>28</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Print">2076-0817</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>7</Issue><PubDate><Year>2020</Year><Month>Jul</Month><Day>16</Day></PubDate></JournalIssue><Title>Pathogens (Basel, Switzerland)</Title><ISOAbbreviation>Pathogens</ISOAbbreviation></Journal><ArticleTitle>Polycystic Kidney Disease Ryanodine Receptor Domain (PKDRR) Proteins in Oomycetes.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">E577</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.3390/pathogens9070577</ELocationID><Abstract><AbstractText>In eukaryotes, two sources of Ca<sup>2+</sup> are accessed to allow rapid changes in the cytosolic levels of this second messenger: the extracellular medium and intracellular Ca<sup>2+</sup> stores, such as the endoplasmic reticulum. One class of channel that permits Ca<sup>2+</sup> entry is the transient receptor potential (TRP) superfamily, including the polycystic kidney disease (PKD) proteins, or polycystins. Channels that release Ca<sup>2+</sup> 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 <i>Phytophthora infestans</i> 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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zheng</LastName><ForeName>Limian</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Department of Physiology, School of Medicine, University College Cork, T12 XF62 Cork, Ireland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Prestwich</LastName><ForeName>Barbara Doyle</ForeName><Initials>BD</Initials><AffiliationInfo><Affiliation>School of Biological, Earth and Environmental Sciences, University College Cork, T23 TK30 Cork, Ireland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Harrison</LastName><ForeName>Patrick T</ForeName><Initials>PT</Initials><Identifier Source="ORCID">0000-0002-2319-0949</Identifier><AffiliationInfo><Affiliation>Department of Physiology, School of Medicine, University College Cork, T12 XF62 Cork, Ireland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mackrill</LastName><ForeName>John J</ForeName><Initials>JJ</Initials><Identifier Source="ORCID">0000-0003-2473-129X</Identifier><AffiliationInfo><Affiliation>Department of Physiology, School of Medicine, University College Cork, T12 XF62 Cork, Ireland.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>07</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Pathogens</MedlineTA><NlmUniqueID>101596317</NlmUniqueID><ISSNLinking>2076-0817</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Phytophthora infestans</Keyword><Keyword MajorTopicYN="N">biochemistry</Keyword><Keyword MajorTopicYN="N">calcium</Keyword><Keyword MajorTopicYN="N">evolution</Keyword><Keyword MajorTopicYN="N">inositol 1,4,5-trisphosphate receptor</Keyword><Keyword MajorTopicYN="N">oomycete</Keyword><Keyword MajorTopicYN="N">polycystic kidney disease channel</Keyword><Keyword MajorTopicYN="N">ryanodine receptor</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>06</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>07</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>07</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>7</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>7</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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(pays)"><noRegion><name sortKey="Zheng, Limian" sort="Zheng, Limian" uniqKey="Zheng L" first="Limian" last="Zheng">Limian Zheng</name></noRegion><name sortKey="Harrison, Patrick T" sort="Harrison, Patrick T" uniqKey="Harrison P" first="Patrick T" last="Harrison">Patrick T. Harrison</name><name sortKey="Mackrill, John J" sort="Mackrill, John J" uniqKey="Mackrill J" first="John J" last="Mackrill">John J. Mackrill</name><name sortKey="Prestwich, Barbara Doyle" sort="Prestwich, Barbara Doyle" uniqKey="Prestwich B" first="Barbara Doyle" last="Prestwich">Barbara Doyle Prestwich</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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