The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation.
Identifieur interne : 001115 ( Ncbi/Curation ); précédent : 001114; suivant : 001116The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation.
Auteurs : Milan Surjit [Inde] ; Ravinder Kumar ; Rabi N. Mishra ; Malireddy K. Reddy ; Vincent T K. Chow ; Sunil K. LalSource :
- Journal of virology [ 0022-538X ] ; 2005.
Descripteurs français
- KwdFr :
- Animaux, Casein Kinase II (métabolisme), Cytoplasme (métabolisme), Glycogen Synthase Kinases (métabolisme), Humains, Isoformes de protéines (métabolisme), Kinases cyclines-dépendantes (métabolisme), Liaison aux protéines, Lignée cellulaire, Membrane cellulaire (métabolisme), Mitogen-Activated Protein Kinases (métabolisme), Noyau de la cellule (métabolisme), Phosphorylation, Protéines 14-3-3 (métabolisme), Protéines nucléocapside (métabolisme), Virus du SRAS (métabolisme).
- MESH :
- métabolisme : Casein Kinase II, Cytoplasme, Glycogen Synthase Kinases, Isoformes de protéines, Kinases cyclines-dépendantes, Membrane cellulaire, Mitogen-Activated Protein Kinases, Noyau de la cellule, Protéines 14-3-3, Protéines nucléocapside, Virus du SRAS.
- Animaux, Humains, Liaison aux protéines, Lignée cellulaire, Phosphorylation.
English descriptors
- KwdEn :
- 14-3-3 Proteins (metabolism), Animals, Casein Kinase II (metabolism), Cell Line, Cell Membrane (metabolism), Cell Nucleus (metabolism), Cyclin-Dependent Kinases (metabolism), Cytoplasm (metabolism), Glycogen Synthase Kinases (metabolism), Humans, Mitogen-Activated Protein Kinases (metabolism), Nucleocapsid Proteins (metabolism), Phosphorylation, Protein Binding, Protein Isoforms (metabolism), SARS Virus (metabolism).
- MESH :
- chemical , metabolism : 14-3-3 Proteins, Casein Kinase II, Cyclin-Dependent Kinases, Glycogen Synthase Kinases, Mitogen-Activated Protein Kinases, Nucleocapsid Proteins, Protein Isoforms.
- metabolism : Cell Membrane, Cell Nucleus, Cytoplasm, SARS Virus.
- Animals, Cell Line, Humans, Phosphorylation, Protein Binding.
Abstract
The severe acute respiratory syndrome coronavirus(SARS-CoV) nucleocapsid (N) protein is one of the four structural proteins of the virus and is predicted to be a 46-kDa phosphoprotein. Our in silico analysis predicted N to be heavily phosphorylated at multiple residues. Experimentally, we have shown in this report that the N protein of the SARS-CoV gets serine-phosphorylated by multiple kinases, in both the cytoplasm and the nucleus. The phosphoprotein is stable and localizes in the cytoplasm and coprecipitates with the membrane fraction. Also, using specific inhibitors of phosphorylation and an in vitro phosphorylation assay, we show that the nucleocapsid protein is a substrate of cyclin-dependent kinase (CDK), glycogen synthase kinase, mitogen-activated protein kinase, and casein kinase II. Further, we show that the phosphorylated protein is translocated to the cytoplasm by binding to 14-3-3 (tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein). 14-3-3 proteins are a family of highly conserved, ubiquitously expressed eukaryotic proteins that function primarily as adapters that modulate interactions between components of various cellular signaling and cell cycle regulatory pathways through phosphorylation-dependent protein-protein interactions. Coincidentally, the N protein was also found to downregulate the expression of the theta isoform of 14-3-3 (14-3-3theta), leading to the accumulation of phosphorylated N protein in the nucleus, in the absence of growth factors. Using short interfering RNA specific to 14-3-3theta we have inhibited its expression to show accumulation of phosphorylated N protein in the nucleus. Thus, the data presented here provide a possible mechanism for phosphorylation-dependent nucleocytoplasmic shuttling of the N protein. This 14-3-3-mediated transport of the phosphorylated N protein and its possible implications in interfering with the cellular machinery are discussed.
DOI: 10.1128/JVI.79.17.11476-11486.2005
PubMed: 16103198
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :002585
- to stream PubMed, to step Curation: Pour aller vers cette notice dans l'étape Curation :002585
- to stream PubMed, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :002415
- to stream Ncbi, to step Merge: Pour aller vers cette notice dans l'étape Curation :001115
Links to Exploration step
pubmed:16103198Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation.</title><author><name sortKey="Surjit, Milan" sort="Surjit, Milan" uniqKey="Surjit M" first="Milan" last="Surjit">Milan Surjit</name><affiliation wicri:level="1"><nlm:affiliation>Virology Group, International Centre for Genetic Engineering & Biotechnology, New Delhi, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Virology Group, International Centre for Genetic Engineering & Biotechnology, New Delhi</wicri:regionArea><wicri:noRegion>New Delhi</wicri:noRegion></affiliation></author><author><name sortKey="Kumar, Ravinder" sort="Kumar, Ravinder" uniqKey="Kumar R" first="Ravinder" last="Kumar">Ravinder Kumar</name></author><author><name sortKey="Mishra, Rabi N" sort="Mishra, Rabi N" uniqKey="Mishra R" first="Rabi N" last="Mishra">Rabi N. Mishra</name></author><author><name sortKey="Reddy, Malireddy K" sort="Reddy, Malireddy K" uniqKey="Reddy M" first="Malireddy K" last="Reddy">Malireddy K. Reddy</name></author><author><name sortKey="Chow, Vincent T K" sort="Chow, Vincent T K" uniqKey="Chow V" first="Vincent T K" last="Chow">Vincent T K. Chow</name></author><author><name sortKey="Lal, Sunil K" sort="Lal, Sunil K" uniqKey="Lal S" first="Sunil K" last="Lal">Sunil K. Lal</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:16103198</idno><idno type="pmid">16103198</idno><idno type="doi">10.1128/JVI.79.17.11476-11486.2005</idno><idno type="wicri:Area/PubMed/Corpus">002585</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002585</idno><idno type="wicri:Area/PubMed/Curation">002585</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002585</idno><idno type="wicri:Area/PubMed/Checkpoint">002415</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002415</idno><idno type="wicri:Area/Ncbi/Merge">001115</idno><idno type="wicri:Area/Ncbi/Curation">001115</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation.</title><author><name sortKey="Surjit, Milan" sort="Surjit, Milan" uniqKey="Surjit M" first="Milan" last="Surjit">Milan Surjit</name><affiliation wicri:level="1"><nlm:affiliation>Virology Group, International Centre for Genetic Engineering & Biotechnology, New Delhi, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Virology Group, International Centre for Genetic Engineering & Biotechnology, New Delhi</wicri:regionArea><wicri:noRegion>New Delhi</wicri:noRegion></affiliation></author><author><name sortKey="Kumar, Ravinder" sort="Kumar, Ravinder" uniqKey="Kumar R" first="Ravinder" last="Kumar">Ravinder Kumar</name></author><author><name sortKey="Mishra, Rabi N" sort="Mishra, Rabi N" uniqKey="Mishra R" first="Rabi N" last="Mishra">Rabi N. Mishra</name></author><author><name sortKey="Reddy, Malireddy K" sort="Reddy, Malireddy K" uniqKey="Reddy M" first="Malireddy K" last="Reddy">Malireddy K. Reddy</name></author><author><name sortKey="Chow, Vincent T K" sort="Chow, Vincent T K" uniqKey="Chow V" first="Vincent T K" last="Chow">Vincent T K. Chow</name></author><author><name sortKey="Lal, Sunil K" sort="Lal, Sunil K" uniqKey="Lal S" first="Sunil K" last="Lal">Sunil K. Lal</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>14-3-3 Proteins (metabolism)</term><term>Animals</term><term>Casein Kinase II (metabolism)</term><term>Cell Line</term><term>Cell Membrane (metabolism)</term><term>Cell Nucleus (metabolism)</term><term>Cyclin-Dependent Kinases (metabolism)</term><term>Cytoplasm (metabolism)</term><term>Glycogen Synthase Kinases (metabolism)</term><term>Humans</term><term>Mitogen-Activated Protein Kinases (metabolism)</term><term>Nucleocapsid Proteins (metabolism)</term><term>Phosphorylation</term><term>Protein Binding</term><term>Protein Isoforms (metabolism)</term><term>SARS Virus (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Casein Kinase II (métabolisme)</term><term>Cytoplasme (métabolisme)</term><term>Glycogen Synthase Kinases (métabolisme)</term><term>Humains</term><term>Isoformes de protéines (métabolisme)</term><term>Kinases cyclines-dépendantes (métabolisme)</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Membrane cellulaire (métabolisme)</term><term>Mitogen-Activated Protein Kinases (métabolisme)</term><term>Noyau de la cellule (métabolisme)</term><term>Phosphorylation</term><term>Protéines 14-3-3 (métabolisme)</term><term>Protéines nucléocapside (métabolisme)</term><term>Virus du SRAS (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>14-3-3 Proteins</term><term>Casein Kinase II</term><term>Cyclin-Dependent Kinases</term><term>Glycogen Synthase Kinases</term><term>Mitogen-Activated Protein Kinases</term><term>Nucleocapsid Proteins</term><term>Protein Isoforms</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Cell Nucleus</term><term>Cytoplasm</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Casein Kinase II</term><term>Cytoplasme</term><term>Glycogen Synthase Kinases</term><term>Isoformes de protéines</term><term>Kinases cyclines-dépendantes</term><term>Membrane cellulaire</term><term>Mitogen-Activated Protein Kinases</term><term>Noyau de la cellule</term><term>Protéines 14-3-3</term><term>Protéines nucléocapside</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Humans</term><term>Phosphorylation</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Phosphorylation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus(SARS-CoV) nucleocapsid (N) protein is one of the four structural proteins of the virus and is predicted to be a 46-kDa phosphoprotein. Our in silico analysis predicted N to be heavily phosphorylated at multiple residues. Experimentally, we have shown in this report that the N protein of the SARS-CoV gets serine-phosphorylated by multiple kinases, in both the cytoplasm and the nucleus. The phosphoprotein is stable and localizes in the cytoplasm and coprecipitates with the membrane fraction. Also, using specific inhibitors of phosphorylation and an in vitro phosphorylation assay, we show that the nucleocapsid protein is a substrate of cyclin-dependent kinase (CDK), glycogen synthase kinase, mitogen-activated protein kinase, and casein kinase II. Further, we show that the phosphorylated protein is translocated to the cytoplasm by binding to 14-3-3 (tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein). 14-3-3 proteins are a family of highly conserved, ubiquitously expressed eukaryotic proteins that function primarily as adapters that modulate interactions between components of various cellular signaling and cell cycle regulatory pathways through phosphorylation-dependent protein-protein interactions. Coincidentally, the N protein was also found to downregulate the expression of the theta isoform of 14-3-3 (14-3-3theta), leading to the accumulation of phosphorylated N protein in the nucleus, in the absence of growth factors. Using short interfering RNA specific to 14-3-3theta we have inhibited its expression to show accumulation of phosphorylated N protein in the nucleus. Thus, the data presented here provide a possible mechanism for phosphorylation-dependent nucleocytoplasmic shuttling of the N protein. This 14-3-3-mediated transport of the phosphorylated N protein and its possible implications in interfering with the cellular machinery are discussed.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Ncbi/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001115 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Curation/biblio.hfd -nk 001115 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= Ncbi
|étape= Curation
|type= RBID
|clé= pubmed:16103198
|texte= The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Curation/RBID.i -Sk "pubmed:16103198" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Curation/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |