Malaria Parasite-Infected Erythrocytes Secrete PfCK1, the Plasmodium Homologue of the Pleiotropic Protein Kinase Casein Kinase 1.
Identifieur interne : 002598 ( PubMed/Corpus ); précédent : 002597; suivant : 002599Malaria Parasite-Infected Erythrocytes Secrete PfCK1, the Plasmodium Homologue of the Pleiotropic Protein Kinase Casein Kinase 1.
Auteurs : Dominique Dorin-Semblat ; Claudia Demarta-Gatsi ; Romain Hamelin ; Florence Armand ; Teresa Gil Carvalho ; Marc Moniatte ; Christian DoerigSource :
- PloS one [ 1932-6203 ] ; 2015.
English descriptors
- KwdEn :
- Blotting, Southern, Blotting, Western, Casein Kinase I (genetics), Casein Kinase I (metabolism), Cloning, Molecular, Erythrocytes (enzymology), Erythrocytes (parasitology), Fluorescent Antibody Technique, Humans, Immunoprecipitation, Malaria (enzymology), Malaria (parasitology), Phosphorylation, Plasmodium falciparum (enzymology), Protozoan Proteins (genetics), Protozoan Proteins (metabolism).
- MESH :
- chemical , genetics : Casein Kinase I, Protozoan Proteins.
- chemical , metabolism : Casein Kinase I, Protozoan Proteins.
- enzymology : Erythrocytes, Malaria, Plasmodium falciparum.
- parasitology : Erythrocytes, Malaria.
- Blotting, Southern, Blotting, Western, Cloning, Molecular, Fluorescent Antibody Technique, Humans, Immunoprecipitation, Phosphorylation.
Abstract
Casein kinase 1 (CK1) is a pleiotropic protein kinase implicated in several fundamental processes of eukaryotic cell biology. Plasmodium falciparum encodes a single CK1 isoform, PfCK1, that is expressed at all stages of the parasite's life cycle. We have previously shown that the pfck1 gene cannot be disrupted, but that the locus can be modified if no loss-of-function is incurred, suggesting an important role for this kinase in intra-erythrocytic asexual proliferation. Here, we report on the use of parasite lines expressing GFP- or His-tagged PfCK1 from the endogenous locus to investigate (i) the dynamics of PfCK1 localisation during the asexual cycle in red blood cells, and (ii) potential interactors of PfCK1, so as to gain insight into the involvement of the enzyme in specific cellular processes. Immunofluorescence analysis reveals a dynamic localisation of PfCK1, with evidence for a pool of the enzyme being directed to the membrane of the host erythrocyte in the early stages of infection, followed by a predominantly intra-parasite localisation in trophozoites and schizonts and association with micronemes in merozoites. Furthermore, we present strong evidence that a pool of enzymatically active PfCK1 is secreted into the culture supernatant, demonstrating that PfCK1 is an ectokinase. Our interactome experiments and ensuing kinase assays using recombinant PfCK1 to phosphorylate putative interactors in vitro suggest an involvement of PfCK1 in many cellular processes such as mRNA splicing, protein trafficking, ribosomal, and host cell invasion.
DOI: 10.1371/journal.pone.0139591
PubMed: 26629826
Links to Exploration step
pubmed:26629826Le document en format XML
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last="Hamelin">Romain Hamelin</name><affiliation><nlm:affiliation>Proteomics Core Facility, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.</nlm:affiliation></affiliation></author><author><name sortKey="Armand, Florence" sort="Armand, Florence" uniqKey="Armand F" first="Florence" last="Armand">Florence Armand</name><affiliation><nlm:affiliation>Proteomics Core Facility, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.</nlm:affiliation></affiliation></author><author><name sortKey="Carvalho, Teresa Gil" sort="Carvalho, Teresa Gil" uniqKey="Carvalho T" first="Teresa Gil" last="Carvalho">Teresa Gil Carvalho</name><affiliation><nlm:affiliation>Infection and Immunity Program, Monash Biomedicine Discovery Institute and Department of Microbiology, Monash University, Victoria, Australia, 3800.</nlm:affiliation></affiliation></author><author><name sortKey="Moniatte, Marc" sort="Moniatte, Marc" uniqKey="Moniatte M" first="Marc" last="Moniatte">Marc 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xml:lang="en">Malaria Parasite-Infected Erythrocytes Secrete PfCK1, the Plasmodium Homologue of the Pleiotropic Protein Kinase Casein Kinase 1.</title><author><name sortKey="Dorin Semblat, Dominique" sort="Dorin Semblat, Dominique" uniqKey="Dorin Semblat D" first="Dominique" last="Dorin-Semblat">Dominique Dorin-Semblat</name><affiliation><nlm:affiliation>UMR S1134, Institut National de Transfusion Sanguine, 6 Rue Alexandre Cabanel, 75015 Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Demarta Gatsi, Claudia" sort="Demarta Gatsi, Claudia" uniqKey="Demarta Gatsi C" first="Claudia" last="Demarta-Gatsi">Claudia Demarta-Gatsi</name><affiliation><nlm:affiliation>Institut Pasteur, Unité de Biologie des Interactions Hôte-Parasites, 25-28 rue du Dr Roux, Paris F-75015, France.</nlm:affiliation></affiliation></author><author><name sortKey="Hamelin, Romain" sort="Hamelin, Romain" uniqKey="Hamelin R" first="Romain" last="Hamelin">Romain Hamelin</name><affiliation><nlm:affiliation>Proteomics Core Facility, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.</nlm:affiliation></affiliation></author><author><name sortKey="Armand, Florence" sort="Armand, Florence" uniqKey="Armand F" first="Florence" last="Armand">Florence Armand</name><affiliation><nlm:affiliation>Proteomics Core Facility, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.</nlm:affiliation></affiliation></author><author><name sortKey="Carvalho, Teresa Gil" sort="Carvalho, Teresa Gil" uniqKey="Carvalho T" first="Teresa Gil" last="Carvalho">Teresa Gil Carvalho</name><affiliation><nlm:affiliation>Infection and Immunity Program, Monash Biomedicine Discovery Institute and Department of Microbiology, Monash University, Victoria, Australia, 3800.</nlm:affiliation></affiliation></author><author><name sortKey="Moniatte, Marc" sort="Moniatte, Marc" uniqKey="Moniatte M" first="Marc" last="Moniatte">Marc Moniatte</name><affiliation><nlm:affiliation>Proteomics Core Facility, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.</nlm:affiliation></affiliation></author><author><name sortKey="Doerig, Christian" sort="Doerig, Christian" uniqKey="Doerig C" first="Christian" last="Doerig">Christian Doerig</name><affiliation><nlm:affiliation>Infection and Immunity Program, Monash Biomedicine Discovery Institute and Department of Microbiology, Monash University, Victoria, Australia, 3800.</nlm:affiliation></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Blotting, Southern</term><term>Blotting, Western</term><term>Casein Kinase I (genetics)</term><term>Casein Kinase I (metabolism)</term><term>Cloning, Molecular</term><term>Erythrocytes (enzymology)</term><term>Erythrocytes (parasitology)</term><term>Fluorescent Antibody Technique</term><term>Humans</term><term>Immunoprecipitation</term><term>Malaria (enzymology)</term><term>Malaria (parasitology)</term><term>Phosphorylation</term><term>Plasmodium falciparum (enzymology)</term><term>Protozoan Proteins (genetics)</term><term>Protozoan Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Casein Kinase I</term><term>Protozoan Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Casein Kinase I</term><term>Protozoan Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Erythrocytes</term><term>Malaria</term><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Erythrocytes</term><term>Malaria</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Blotting, Southern</term><term>Blotting, Western</term><term>Cloning, Molecular</term><term>Fluorescent Antibody Technique</term><term>Humans</term><term>Immunoprecipitation</term><term>Phosphorylation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Casein kinase 1 (CK1) is a pleiotropic protein kinase implicated in several fundamental processes of eukaryotic cell biology. Plasmodium falciparum encodes a single CK1 isoform, PfCK1, that is expressed at all stages of the parasite's life cycle. We have previously shown that the pfck1 gene cannot be disrupted, but that the locus can be modified if no loss-of-function is incurred, suggesting an important role for this kinase in intra-erythrocytic asexual proliferation. Here, we report on the use of parasite lines expressing GFP- or His-tagged PfCK1 from the endogenous locus to investigate (i) the dynamics of PfCK1 localisation during the asexual cycle in red blood cells, and (ii) potential interactors of PfCK1, so as to gain insight into the involvement of the enzyme in specific cellular processes. Immunofluorescence analysis reveals a dynamic localisation of PfCK1, with evidence for a pool of the enzyme being directed to the membrane of the host erythrocyte in the early stages of infection, followed by a predominantly intra-parasite localisation in trophozoites and schizonts and association with micronemes in merozoites. Furthermore, we present strong evidence that a pool of enzymatically active PfCK1 is secreted into the culture supernatant, demonstrating that PfCK1 is an ectokinase. Our interactome experiments and ensuing kinase assays using recombinant PfCK1 to phosphorylate putative interactors in vitro suggest an involvement of PfCK1 in many cellular processes such as mRNA splicing, protein trafficking, ribosomal, and host cell invasion.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26629826</PMID><DateCreated><Year>2015</Year><Month>12</Month><Day>03</Day></DateCreated><DateCompleted><Year>2016</Year><Month>06</Month><Day>23</Day></DateCompleted><DateRevised><Year>2015</Year><Month>12</Month><Day>14</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>10</Volume><Issue>12</Issue><PubDate><Year>2015</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>Malaria Parasite-Infected Erythrocytes Secrete PfCK1, the Plasmodium Homologue of the Pleiotropic Protein Kinase Casein Kinase 1.</ArticleTitle><Pagination><MedlinePgn>e0139591</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0139591</ELocationID><Abstract><AbstractText>Casein kinase 1 (CK1) is a pleiotropic protein kinase implicated in several fundamental processes of eukaryotic cell biology. Plasmodium falciparum encodes a single CK1 isoform, PfCK1, that is expressed at all stages of the parasite's life cycle. We have previously shown that the pfck1 gene cannot be disrupted, but that the locus can be modified if no loss-of-function is incurred, suggesting an important role for this kinase in intra-erythrocytic asexual proliferation. Here, we report on the use of parasite lines expressing GFP- or His-tagged PfCK1 from the endogenous locus to investigate (i) the dynamics of PfCK1 localisation during the asexual cycle in red blood cells, and (ii) potential interactors of PfCK1, so as to gain insight into the involvement of the enzyme in specific cellular processes. Immunofluorescence analysis reveals a dynamic localisation of PfCK1, with evidence for a pool of the enzyme being directed to the membrane of the host erythrocyte in the early stages of infection, followed by a predominantly intra-parasite localisation in trophozoites and schizonts and association with micronemes in merozoites. Furthermore, we present strong evidence that a pool of enzymatically active PfCK1 is secreted into the culture supernatant, demonstrating that PfCK1 is an ectokinase. Our interactome experiments and ensuing kinase assays using recombinant PfCK1 to phosphorylate putative interactors in vitro suggest an involvement of PfCK1 in many cellular processes such as mRNA splicing, protein trafficking, ribosomal, and host cell invasion.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dorin-Semblat</LastName><ForeName>Dominique</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>UMR S1134, Institut National de Transfusion Sanguine, 6 Rue Alexandre Cabanel, 75015 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Demarta-Gatsi</LastName><ForeName>Claudia</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Institut Pasteur, Unité de Biologie des Interactions Hôte-Parasites, 25-28 rue du Dr Roux, Paris F-75015, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hamelin</LastName><ForeName>Romain</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Proteomics Core Facility, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Armand</LastName><ForeName>Florence</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Proteomics Core Facility, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Carvalho</LastName><ForeName>Teresa Gil</ForeName><Initials>TG</Initials><AffiliationInfo><Affiliation>Infection and Immunity Program, Monash Biomedicine Discovery Institute and Department of Microbiology, Monash University, Victoria, Australia, 3800.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Moniatte</LastName><ForeName>Marc</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Proteomics Core Facility, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Doerig</LastName><ForeName>Christian</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Infection and Immunity Program, Monash Biomedicine Discovery Institute and Department of Microbiology, Monash University, Victoria, Australia, 3800.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>12</Month><Day>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS 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Chem. 1997 Dec 5;272(49):30760-5</RefSource><PMID Version="1">9388215</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D015139" MajorTopicYN="N">Blotting, Southern</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047389" MajorTopicYN="N">Casein Kinase I</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004912" MajorTopicYN="N">Erythrocytes</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000469" MajorTopicYN="N">parasitology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005455" MajorTopicYN="N">Fluorescent Antibody Technique</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047468" MajorTopicYN="N">Immunoprecipitation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008288" MajorTopicYN="N">Malaria</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000469" MajorTopicYN="N">parasitology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010963" MajorTopicYN="N">Plasmodium falciparum</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015800" MajorTopicYN="N">Protozoan Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4668060</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>07</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>09</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>12</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>12</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>6</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26629826</ArticleId><ArticleId IdType="doi">10.1371/journal.pone.0139591</ArticleId><ArticleId IdType="pii">PONE-D-15-32114</ArticleId><ArticleId 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