14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma 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, 14-3-3ζ, is believed to function in cell signaling, cycle contro...

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Autores principales:	Jia Zhang, Fangjin Chen, Wenliang Li, Qian Xiong, Mingkun Yang, Peng Zheng, Chongyang Li, Jianfeng Pei, Feng Ge
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/de5ae50d3b9643bb9cb6f374d0007f3a
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spelling	oai:doaj.org-article:de5ae50d3b9643bb9cb6f374d0007f3a2021-11-18T07:29:59Z14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma cells.1932-620310.1371/journal.pone.0029554https://doaj.org/article/de5ae50d3b9643bb9cb6f374d0007f3a2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22279540/?tool=EBIhttps://doaj.org/toc/1932-6203The 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, 14-3-3ζ, 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 14-3-3ζ interacting protein. Following our initial finding, in this study, we provide evidence that 14-3-3ζ interacts physically with Stat3. We further demonstrate that phosphorylation of Stat3 at Ser727 is vital for 14-3-3ζ interaction and mutation of Ser727 to Alanine abolished 14-3-3ζ/Stat3 association. Inhibition of 14-3-3ζ protein expression in U266 cells inhibited Stat3 Ser727 phosphorylation and nuclear translocation, and decreased both Stat3 DNA binding and transcriptional activity. Moreover, 14-3-3ζ is involved in the regulation of protein kinase C (PKC) activity and 14-3-3ζ 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 14-3-3ζ serves as an essential coordinator for different pathways to regulate Stat3 activation and function in MM cells.Jia ZhangFangjin ChenWenliang LiQian XiongMingkun YangPeng ZhengChongyang LiJianfeng PeiFeng GePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 1, p e29554 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jia Zhang Fangjin Chen Wenliang Li Qian Xiong Mingkun Yang Peng Zheng Chongyang Li Jianfeng Pei Feng Ge 14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma cells.
description	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, 14-3-3ζ, 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 14-3-3ζ interacting protein. Following our initial finding, in this study, we provide evidence that 14-3-3ζ interacts physically with Stat3. We further demonstrate that phosphorylation of Stat3 at Ser727 is vital for 14-3-3ζ interaction and mutation of Ser727 to Alanine abolished 14-3-3ζ/Stat3 association. Inhibition of 14-3-3ζ protein expression in U266 cells inhibited Stat3 Ser727 phosphorylation and nuclear translocation, and decreased both Stat3 DNA binding and transcriptional activity. Moreover, 14-3-3ζ is involved in the regulation of protein kinase C (PKC) activity and 14-3-3ζ 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 14-3-3ζ serves as an essential coordinator for different pathways to regulate Stat3 activation and function in MM cells.
format	article
author	Jia Zhang Fangjin Chen Wenliang Li Qian Xiong Mingkun Yang Peng Zheng Chongyang Li Jianfeng Pei Feng Ge
author_facet	Jia Zhang Fangjin Chen Wenliang Li Qian Xiong Mingkun Yang Peng Zheng Chongyang Li Jianfeng Pei Feng Ge
author_sort	Jia Zhang
title	14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma cells.
title_short	14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma cells.
title_full	14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma cells.
title_fullStr	14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma cells.
title_full_unstemmed	14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma cells.
title_sort	14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma cells.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/de5ae50d3b9643bb9cb6f374d0007f3a
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14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma cells.

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