author_facet Fu, Jing
Yang, Ziqiang
Wei, Jinxue
Han, Jiahuai
Gu, Jun
Fu, Jing
Yang, Ziqiang
Wei, Jinxue
Han, Jiahuai
Gu, Jun
author Fu, Jing
Yang, Ziqiang
Wei, Jinxue
Han, Jiahuai
Gu, Jun
spellingShingle Fu, Jing
Yang, Ziqiang
Wei, Jinxue
Han, Jiahuai
Gu, Jun
Journal of Cell Science
Nuclear protein NP60 regulates p38 MAPK activity
Cell Biology
author_sort fu, jing
spelling Fu, Jing Yang, Ziqiang Wei, Jinxue Han, Jiahuai Gu, Jun 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.02699 <jats:p>The activation of p38α is mediated by its upstream kinase and associated proteins. Here we identify a new nuclear protein, NP60, which regulates the activation of p38α in response to sorbitol treatment. NP60 specifically binds to p38α, but not to JNK and ERK, in vitro and in vivo. Co-transfection of NP60 leads to the phosphorylation and activation of p38α, and subsequently results in the phosphorylation and activation of activating transcription factor 2. The phosphorylation of p38α induced by NP60 requires upstream activity of p38α MAP kinase, MAP kinase kinase 6 (MKK6) or MKK4. Our results indicate that NP60 mediates stress activation of p38α and regulates p38α signaling in a specific way.</jats:p> Nuclear protein NP60 regulates p38 MAPK activity Journal of Cell Science
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title Nuclear protein NP60 regulates p38 MAPK activity
title_unstemmed Nuclear protein NP60 regulates p38 MAPK activity
title_full Nuclear protein NP60 regulates p38 MAPK activity
title_fullStr Nuclear protein NP60 regulates p38 MAPK activity
title_full_unstemmed Nuclear protein NP60 regulates p38 MAPK activity
title_short Nuclear protein NP60 regulates p38 MAPK activity
title_sort nuclear protein np60 regulates p38 mapk activity
topic Cell Biology
url http://dx.doi.org/10.1242/jcs.02699
publishDate 2006
physical 115-123
description <jats:p>The activation of p38α is mediated by its upstream kinase and associated proteins. Here we identify a new nuclear protein, NP60, which regulates the activation of p38α in response to sorbitol treatment. NP60 specifically binds to p38α, but not to JNK and ERK, in vitro and in vivo. Co-transfection of NP60 leads to the phosphorylation and activation of p38α, and subsequently results in the phosphorylation and activation of activating transcription factor 2. The phosphorylation of p38α induced by NP60 requires upstream activity of p38α MAP kinase, MAP kinase kinase 6 (MKK6) or MKK4. Our results indicate that NP60 mediates stress activation of p38α and regulates p38α signaling in a specific way.</jats:p>
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author Fu, Jing, Yang, Ziqiang, Wei, Jinxue, Han, Jiahuai, Gu, Jun
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description <jats:p>The activation of p38α is mediated by its upstream kinase and associated proteins. Here we identify a new nuclear protein, NP60, which regulates the activation of p38α in response to sorbitol treatment. NP60 specifically binds to p38α, but not to JNK and ERK, in vitro and in vivo. Co-transfection of NP60 leads to the phosphorylation and activation of p38α, and subsequently results in the phosphorylation and activation of activating transcription factor 2. The phosphorylation of p38α induced by NP60 requires upstream activity of p38α MAP kinase, MAP kinase kinase 6 (MKK6) or MKK4. Our results indicate that NP60 mediates stress activation of p38α and regulates p38α signaling in a specific way.</jats:p>
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spelling Fu, Jing Yang, Ziqiang Wei, Jinxue Han, Jiahuai Gu, Jun 1477-9137 0021-9533 The Company of Biologists Cell Biology http://dx.doi.org/10.1242/jcs.02699 <jats:p>The activation of p38α is mediated by its upstream kinase and associated proteins. Here we identify a new nuclear protein, NP60, which regulates the activation of p38α in response to sorbitol treatment. NP60 specifically binds to p38α, but not to JNK and ERK, in vitro and in vivo. Co-transfection of NP60 leads to the phosphorylation and activation of p38α, and subsequently results in the phosphorylation and activation of activating transcription factor 2. The phosphorylation of p38α induced by NP60 requires upstream activity of p38α MAP kinase, MAP kinase kinase 6 (MKK6) or MKK4. Our results indicate that NP60 mediates stress activation of p38α and regulates p38α signaling in a specific way.</jats:p> Nuclear protein NP60 regulates p38 MAPK activity Journal of Cell Science
spellingShingle Fu, Jing, Yang, Ziqiang, Wei, Jinxue, Han, Jiahuai, Gu, Jun, Journal of Cell Science, Nuclear protein NP60 regulates p38 MAPK activity, Cell Biology
title Nuclear protein NP60 regulates p38 MAPK activity
title_full Nuclear protein NP60 regulates p38 MAPK activity
title_fullStr Nuclear protein NP60 regulates p38 MAPK activity
title_full_unstemmed Nuclear protein NP60 regulates p38 MAPK activity
title_short Nuclear protein NP60 regulates p38 MAPK activity
title_sort nuclear protein np60 regulates p38 mapk activity
title_unstemmed Nuclear protein NP60 regulates p38 MAPK activity
topic Cell Biology
url http://dx.doi.org/10.1242/jcs.02699