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Nuclear protein NP60 regulates p38 MAPK activity
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Zeitschriftentitel: | Journal of Cell Science |
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Personen und Körperschaften: | , , , , |
In: | Journal of Cell Science, 119, 2006, 1, S. 115-123 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
The Company of Biologists
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Schlagwörter: |
author_facet |
Fu, Jing Yang, Ziqiang Wei, Jinxue Han, Jiahuai Gu, Jun Fu, Jing Yang, Ziqiang Wei, Jinxue Han, Jiahuai Gu, Jun |
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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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10.1242/jcs.02699 |
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The Company of Biologists, 2006 |
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The Company of Biologists, 2006 |
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2006 |
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The Company of Biologists |
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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 |
author_facet | Fu, Jing, Yang, Ziqiang, Wei, Jinxue, Han, Jiahuai, Gu, Jun, Fu, Jing, Yang, Ziqiang, Wei, Jinxue, Han, Jiahuai, Gu, Jun |
author_sort | fu, jing |
container_issue | 1 |
container_start_page | 115 |
container_title | Journal of Cell Science |
container_volume | 119 |
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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imprint | The Company of Biologists, 2006 |
imprint_str_mv | The Company of Biologists, 2006 |
institution | DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1 |
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series | Journal of Cell Science |
source_id | 49 |
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 |