The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation.
Identifieur interne : 002585 ( PubMed/Curation ); précédent : 002584; suivant : 002586The 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
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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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16103198</PMID><DateCompleted><Year>2005</Year><Month>09</Month><Day>29</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-538X</ISSN><JournalIssue CitedMedium="Print"><Volume>79</Volume><Issue>17</Issue><PubDate><Year>2005</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>The severe acute respiratory syndrome coronavirus nucleocapsid protein is phosphorylated and localizes in the cytoplasm by 14-3-3-mediated translocation.</ArticleTitle><Pagination><MedlinePgn>11476-86</MedlinePgn></Pagination><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Surjit</LastName><ForeName>Milan</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Virology Group, International Centre for Genetic Engineering & Biotechnology, New Delhi, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kumar</LastName><ForeName>Ravinder</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Mishra</LastName><ForeName>Rabi N</ForeName><Initials>RN</Initials></Author><Author ValidYN="Y"><LastName>Reddy</LastName><ForeName>Malireddy K</ForeName><Initials>MK</Initials></Author><Author ValidYN="Y"><LastName>Chow</LastName><ForeName>Vincent T K</ForeName><Initials>VT</Initials></Author><Author ValidYN="Y"><LastName>Lal</LastName><ForeName>Sunil K</ForeName><Initials>SK</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Virol</MedlineTA><NlmUniqueID>0113724</NlmUniqueID><ISSNLinking>0022-538X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D048948">14-3-3 Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019590">Nucleocapsid Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020033">Protein Isoforms</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C099602">nucleocapsid protein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 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