IHB OpenIR  > 水生生物分子与细胞生物学研究中心  > 期刊论文
14-3-3 zeta Interacts with Stat3 and Regulates Its Constitutive Activation in Multiple Myeloma Cells
Zhang, Jia1; Chen, Fangjin2; Li, Wenliang3; Xiong, Qian1; Yang, Mingkun1; Zheng, Peng1; Li, Chongyang1; Pei, Jianfeng2; Ge, Feng1; Zhang, J (reprint author), Chinese Acad Sci, Inst Hydrobiol, Wuhan, Peoples R China
2012-01-18
Source PublicationPLOS ONE
ISSN1932-6203
Volume7Issue:1Pages:e29554
AbstractThe 14-3-3 proteins are a family of regulatory signaling molecules that interact with other proteins in a phosphorylation-dependent manner and function as adapter or scaffold proteins in signal transduction pathways. One family member, 14-3-3 zeta, is believed to function in cell signaling, cycle control, and apoptotic death. A systematic proteomic analysis done in our laboratory has identified signal transducers and activators of transcription 3 (Stat3) as a novel 14-3-3 zeta interacting protein. Following our initial finding, in this study, we provide evidence that 14-3-3 zeta interacts physically with Stat3. We further demonstrate that phosphorylation of Stat3 at Ser727 is vital for 14-3-3 zeta interaction and mutation of Ser727 to Alanine abolished 14-3-3 zeta/Stat3 association. Inhibition of 14-3-3 zeta protein expression in U266 cells inhibited Stat3 Ser727 phosphorylation and nuclear translocation, and decreased both Stat3 DNA binding and transcriptional activity. Moreover, 14-3-3 zeta is involved in the regulation of protein kinase C (PKC) activity and 14-3-3 zeta binding to Stat3 protects Ser727 dephosphorylation from protein phosphatase 2A (PP2A). Taken together, our findings support the model that multiple signaling events impinge on Stat3 and that 14-3-3 zeta serves as an essential coordinator for different pathways to regulate Stat3 activation and function in MM cells.; The 14-3-3 proteins are a family of regulatory signaling molecules that interact with other proteins in a phosphorylation-dependent manner and function as adapter or scaffold proteins in signal transduction pathways. One family member, 14-3-3 zeta, is believed to function in cell signaling, cycle control, and apoptotic death. A systematic proteomic analysis done in our laboratory has identified signal transducers and activators of transcription 3 (Stat3) as a novel 14-3-3 zeta interacting protein. Following our initial finding, in this study, we provide evidence that 14-3-3 zeta interacts physically with Stat3. We further demonstrate that phosphorylation of Stat3 at Ser727 is vital for 14-3-3 zeta interaction and mutation of Ser727 to Alanine abolished 14-3-3 zeta/Stat3 association. Inhibition of 14-3-3 zeta protein expression in U266 cells inhibited Stat3 Ser727 phosphorylation and nuclear translocation, and decreased both Stat3 DNA binding and transcriptional activity. Moreover, 14-3-3 zeta is involved in the regulation of protein kinase C (PKC) activity and 14-3-3 zeta binding to Stat3 protects Ser727 dephosphorylation from protein phosphatase 2A (PP2A). Taken together, our findings support the model that multiple signaling events impinge on Stat3 and that 14-3-3 zeta serves as an essential coordinator for different pathways to regulate Stat3 activation and function in MM cells.
SubtypeArticle
Department[Zhang, Jia; Xiong, Qian; Yang, Mingkun; Zheng, Peng; Li, Chongyang; Ge, Feng] Chinese Acad Sci, Inst Hydrobiol, Wuhan, Peoples R China; [Chen, Fangjin; Pei, Jianfeng] Peking Univ, Ctr Theoret Biol, Acad Adv Interdisciplinary Studies, Beijing 100871, Peoples R China; [Li, Wenliang] Tokai Univ, Sch Sci & Technol, Tokyo 151, Japan
DOI10.1371/journal.pone.0029554
WOS HeadingsScience & Technology
Funding OrganizationChinese Academy of Sciences; Japan Society for the Promotion of Science ; Chinese Academy of Sciences; Japan Society for the Promotion of Science ; Chinese Academy of Sciences; Japan Society for the Promotion of Science ; Chinese Academy of Sciences; Japan Society for the Promotion of Science
Indexed BySCI
Language英语
WOS Research AreaScience & Technology - Other Topics
WOS SubjectMultidisciplinary Sciences
WOS IDWOS:000299771900018
WOS KeywordPROTEIN-KINASE-C ; PHOSPHORYLATION-DEPENDENT BINDING ; MM-PBSA METHOD ; IN-VIVO ; PROSTATE-CANCER ; PHOSPHATASE 2A ; APOPTOSIS ; RAF-1 ; 14-3-3-PROTEINS ; IDENTIFICATION
Funding OrganizationChinese Academy of Sciences; Japan Society for the Promotion of Science ; Chinese Academy of Sciences; Japan Society for the Promotion of Science ; Chinese Academy of Sciences; Japan Society for the Promotion of Science ; Chinese Academy of Sciences; Japan Society for the Promotion of Science
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Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/16765
Collection水生生物分子与细胞生物学研究中心_期刊论文
Corresponding AuthorZhang, J (reprint author), Chinese Acad Sci, Inst Hydrobiol, Wuhan, Peoples R China
Affiliation1.Chinese Acad Sci, Inst Hydrobiol, Wuhan, Peoples R China
2.Peking Univ, Ctr Theoret Biol, Acad Adv Interdisciplinary Studies, Beijing 100871, Peoples R China
3.Tokai Univ, Sch Sci & Technol, Tokyo 151, Japan
Recommended Citation
GB/T 7714
Zhang, Jia,Chen, Fangjin,Li, Wenliang,et al. 14-3-3 zeta Interacts with Stat3 and Regulates Its Constitutive Activation in Multiple Myeloma Cells[J]. PLOS ONE,2012,7(1):e29554.
APA Zhang, Jia.,Chen, Fangjin.,Li, Wenliang.,Xiong, Qian.,Yang, Mingkun.,...&Zhang, J .(2012).14-3-3 zeta Interacts with Stat3 and Regulates Its Constitutive Activation in Multiple Myeloma Cells.PLOS ONE,7(1),e29554.
MLA Zhang, Jia,et al."14-3-3 zeta Interacts with Stat3 and Regulates Its Constitutive Activation in Multiple Myeloma Cells".PLOS ONE 7.1(2012):e29554.
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