Tyrosine dephosphorylation of STAT3 in SARS coronavirus-infected Vero E6 cells.
Identifieur interne : 004F93 ( Main/Exploration ); précédent : 004F92; suivant : 004F94Tyrosine dephosphorylation of STAT3 in SARS coronavirus-infected Vero E6 cells.
Auteurs : Tetsuya Mizutani [Japon] ; Shuetsu Fukushi ; Masaaki Murakami ; Toshio Hirano ; Masayuki Saijo ; Ichiro Kurane ; Shigeru MorikawaSource :
- FEBS letters [ 0014-5793 ] ; 2004.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : DNA-Binding Proteins, Mitogen-Activated Protein Kinases, Trans-Activators, Tyrosine.
- metabolism : Cell Nucleus, SARS Virus.
- Animals, Chlorocebus aethiops, Phosphorylation, STAT3 Transcription Factor, Vero Cells.
Abstract
Severe acute respiratory syndrome (SARS) has become a global public health emergency. p38 mitogen-activated protein kinase (MAPK) and its downstream targets are activated in SARS coronavirus (SARS-CoV)-infected Vero E6 cells and activation of p38 MAPK enhances the cytopathic effects of SARS-CoV infection. In addition, weak activation of Akt cannot prevent SARS-CoV infection-induced apoptosis in Vero E6 cells. In the present study, we demonstrated that signal transducer and activator of transcription (STAT) 3, which is constitutively phosphorylated at tyrosine (Tyr)-705 and slightly phosphorylated at serine (Ser)-727 in Vero E6 cells, was dephosphorylated at Tyr-705 on SARS-CoV infection. In addition to phosphorylation of p38 MAPK in virus-infected cells, other MAPKs, i.e., extracellular signal-regulated kinase (ERK) 1/2 and c-Jun N-terminal kinase (JNK), were phosphorylated. Although inhibitors of ERK1/2 and JNK (PD98059 and SP600125) had no effect on phosphorylation status of STAT3, inhibitors of p38 MAPK (SB203580 and SB202190) partially inhibited dephosphorylation of STAT3 at Tyr-705. Tyr-705-phosphorylated STAT3 was localized mainly in the nucleus in mock infected cells, whereas STAT3 disappeared from the nucleus in virus-infected cells. As STAT3 acts as an activator of transcription in the nucleus, these results suggest that STAT3 lacks its activity on transcription in SARS-CoV-infected Vero E6 cells.
DOI: 10.1016/j.febslet.2004.10.005
PubMed: 15527783
Affiliations:
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Le document en format XML
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<term>Chlorocebus aethiops</term>
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<term>Mitogen-Activated Protein Kinases (metabolism)</term>
<term>Phosphorylation</term>
<term>SARS Virus (metabolism)</term>
<term>STAT3 Transcription Factor</term>
<term>Trans-Activators (metabolism)</term>
<term>Tyrosine (metabolism)</term>
<term>Vero Cells</term>
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<term>Transactivateurs (métabolisme)</term>
<term>Tyrosine (métabolisme)</term>
<term>Virus du SRAS (métabolisme)</term>
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<term>Protéines de liaison à l'ADN</term>
<term>Transactivateurs</term>
<term>Tyrosine</term>
<term>Virus du SRAS</term>
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<term>Cellules Vero</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) has become a global public health emergency. p38 mitogen-activated protein kinase (MAPK) and its downstream targets are activated in SARS coronavirus (SARS-CoV)-infected Vero E6 cells and activation of p38 MAPK enhances the cytopathic effects of SARS-CoV infection. In addition, weak activation of Akt cannot prevent SARS-CoV infection-induced apoptosis in Vero E6 cells. In the present study, we demonstrated that signal transducer and activator of transcription (STAT) 3, which is constitutively phosphorylated at tyrosine (Tyr)-705 and slightly phosphorylated at serine (Ser)-727 in Vero E6 cells, was dephosphorylated at Tyr-705 on SARS-CoV infection. In addition to phosphorylation of p38 MAPK in virus-infected cells, other MAPKs, i.e., extracellular signal-regulated kinase (ERK) 1/2 and c-Jun N-terminal kinase (JNK), were phosphorylated. Although inhibitors of ERK1/2 and JNK (PD98059 and SP600125) had no effect on phosphorylation status of STAT3, inhibitors of p38 MAPK (SB203580 and SB202190) partially inhibited dephosphorylation of STAT3 at Tyr-705. Tyr-705-phosphorylated STAT3 was localized mainly in the nucleus in mock infected cells, whereas STAT3 disappeared from the nucleus in virus-infected cells. As STAT3 acts as an activator of transcription in the nucleus, these results suggest that STAT3 lacks its activity on transcription in SARS-CoV-infected Vero E6 cells.</div>
</front>
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<name sortKey="Hirano, Toshio" sort="Hirano, Toshio" uniqKey="Hirano T" first="Toshio" last="Hirano">Toshio Hirano</name>
<name sortKey="Kurane, Ichiro" sort="Kurane, Ichiro" uniqKey="Kurane I" first="Ichiro" last="Kurane">Ichiro Kurane</name>
<name sortKey="Morikawa, Shigeru" sort="Morikawa, Shigeru" uniqKey="Morikawa S" first="Shigeru" last="Morikawa">Shigeru Morikawa</name>
<name sortKey="Murakami, Masaaki" sort="Murakami, Masaaki" uniqKey="Murakami M" first="Masaaki" last="Murakami">Masaaki Murakami</name>
<name sortKey="Saijo, Masayuki" sort="Saijo, Masayuki" uniqKey="Saijo M" first="Masayuki" last="Saijo">Masayuki Saijo</name>
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<country name="Japon"><region name="Région de Kantō"><name sortKey="Mizutani, Tetsuya" sort="Mizutani, Tetsuya" uniqKey="Mizutani T" first="Tetsuya" last="Mizutani">Tetsuya Mizutani</name>
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