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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2011-5-4
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pubmed:abstractText |
The oncoprotein c-Jun is one of the components of the activator protein-1 (AP-1) transcription factor complex. AP-1 regulates the expression of many genes and is involved in a variety of biological functions such as cell transformation, proliferation, differentiation and apoptosis. AP-1 activates a variety of tumor-related genes and therefore promotes tumorigenesis and malignant transformation. Here, we found that epidermal growth factor (EGF) induces phosphorylation of c-Jun by P21-activated kinase (PAK) 2. Our data showed that PAK2 binds and phosphorylates c-Jun at five threonine sites (Thr2, Thr8, Thr89, Thr93 and Thr286) in vitro and ex vivo. Knockdown of PAK2 in JB6 Cl41 (P+) cells had no effect on c-Jun phosphorylation at Ser63 or Ser73 but resulted in decreases in EGF-induced anchorage-independent cell transformation, proliferation and AP-1 activity. Mutation at all five c-Jun threonine sites phosphorylated by PAK2 decreased the transforming ability of JB6 cells. Knockdown of PAK2 in SK-MEL-5 melanoma cells also decreased colony formation, proliferation and AP-1 activity. These results indicated that PAK2/c-Jun signaling plays an important role in EGF-induced cell proliferation and transformation.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1460-2180
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pubmed:author |
pubmed-author:BodeAnn MAM,
pubmed-author:DongZigangZ,
pubmed-author:DongZimingZ,
pubmed-author:LiTingtingT,
pubmed-author:LiXiangX,
pubmed-author:LiuKangdongK,
pubmed-author:MaWeiyaW,
pubmed-author:PengCongC,
pubmed-author:ShiGuozhengG,
pubmed-author:WenWeihongW,
pubmed-author:ZhangJishuaiJ,
pubmed-author:ZhuFengF,
pubmed-author:ZykovaTatyanaT
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pubmed:issnType |
Electronic
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
659-66
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pubmed:meshHeading |
pubmed-meshheading:21177766-Animals,
pubmed-meshheading:21177766-Blotting, Western,
pubmed-meshheading:21177766-Cell Proliferation,
pubmed-meshheading:21177766-Cell Transformation, Neoplastic,
pubmed-meshheading:21177766-Cells, Cultured,
pubmed-meshheading:21177766-Epidermal Growth Factor,
pubmed-meshheading:21177766-Epidermis,
pubmed-meshheading:21177766-Humans,
pubmed-meshheading:21177766-Immunoenzyme Techniques,
pubmed-meshheading:21177766-Immunoprecipitation,
pubmed-meshheading:21177766-Melanoma,
pubmed-meshheading:21177766-Mice,
pubmed-meshheading:21177766-Mutation,
pubmed-meshheading:21177766-Phosphorylation,
pubmed-meshheading:21177766-Proto-Oncogene Proteins c-jun,
pubmed-meshheading:21177766-RNA, Small Interfering,
pubmed-meshheading:21177766-Skin,
pubmed-meshheading:21177766-Skin Neoplasms,
pubmed-meshheading:21177766-Threonine,
pubmed-meshheading:21177766-Tissue Array Analysis,
pubmed-meshheading:21177766-Transcription Factor AP-1,
pubmed-meshheading:21177766-p21-Activated Kinases
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pubmed:year |
2011
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pubmed:articleTitle |
P21-activated protein kinase (PAK2)-mediated c-Jun phosphorylation at 5 threonine sites promotes cell transformation.
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pubmed:affiliation |
The Hormel Institute, University of Minnesota, 801 16th Avenue North East, Austin, MN 55912, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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