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Ran binding protein 9(RanBPM) binds IFN-λR1 in the IFN-λsignaling pathway
Like the type I interferons(IFNs),the recently discovered cytokine IFN-λ displays antiviral,antiproliferative,and proapoptotic activities,mediated by a heterodimeric IFN-λ receptor complex composed of a unique IFN-λR1 chain and the IL-10R2 chain.However,the molecular mechanism of the IFN-λ-regulated...
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Published in: | 中国科学:生命科学英文版 2017, Vol.60 (9), p.1030-1039 |
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container_title | 中国科学:生命科学英文版 |
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creator | Junwen Zhang XiaojieCong Jiajie Zhaoqiao Xia Yang Meng Li Hong Chen Ruifang Mi Guishan Jin Fusheng Liu Bing-Ren Huang |
description | Like the type I interferons(IFNs),the recently discovered cytokine IFN-λ displays antiviral,antiproliferative,and proapoptotic activities,mediated by a heterodimeric IFN-λ receptor complex composed of a unique IFN-λR1 chain and the IL-10R2 chain.However,the molecular mechanism of the IFN-λ-regulated pathway remains unclear.In this study,we newly identified RAN-binding protein M(RanBPM) as a binding partner of IFN-λR1.The interaction between RanBPM and IFN-λRl was identified with a glutathione S-transferase pull-down assay and coimmunoprecipitation experiments.IFN-λ1 stimulates this interaction and affects the cellular distribution of RanBPM.However,the interaction between RanBPM and IFN-λR1 does not correlate with their conserved TRAF6-binding sites.Furthermore,we also found that RanBPM is a scaffolding protein with a modulatory function that regulates the activities of IFN-stimulated response elements.Therefore,RanBPM plays a novel role in the IFN-λ-regulated signaling pathway. |
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Zhaoqiao Xia Yang Meng Li Hong Chen Ruifang Mi Guishan Jin Fusheng Liu Bing-Ren Huang</creatorcontrib><description>Like the type I interferons(IFNs),the recently discovered cytokine IFN-λ displays antiviral,antiproliferative,and proapoptotic activities,mediated by a heterodimeric IFN-λ receptor complex composed of a unique IFN-λR1 chain and the IL-10R2 chain.However,the molecular mechanism of the IFN-λ-regulated pathway remains unclear.In this study,we newly identified RAN-binding protein M(RanBPM) as a binding partner of IFN-λR1.The interaction between RanBPM and IFN-λRl was identified with a glutathione S-transferase pull-down assay and coimmunoprecipitation experiments.IFN-λ1 stimulates this interaction and affects the cellular distribution of RanBPM.However,the interaction between RanBPM and IFN-λR1 does not correlate with their conserved TRAF6-binding sites.Furthermore,we also found that RanBPM is a scaffolding protein with a modulatory function that regulates the activities of 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type I interferons(IFNs),the recently discovered cytokine IFN-λ displays antiviral,antiproliferative,and proapoptotic activities,mediated by a heterodimeric IFN-λ receptor complex composed of a unique IFN-λR1 chain and the IL-10R2 chain.However,the molecular mechanism of the IFN-λ-regulated pathway remains unclear.In this study,we newly identified RAN-binding protein M(RanBPM) as a binding partner of IFN-λR1.The interaction between RanBPM and IFN-λRl was identified with a glutathione S-transferase pull-down assay and coimmunoprecipitation experiments.IFN-λ1 stimulates this interaction and affects the cellular distribution of RanBPM.However,the interaction between RanBPM and IFN-λR1 does not correlate with their conserved TRAF6-binding sites.Furthermore,we also found that RanBPM is a scaffolding protein with a modulatory function that regulates the activities of IFN-stimulated response elements.Therefore,RanBPM plays a novel role in the IFN-λ-regulated signaling pathway.</description><subject>IFN-γ</subject><subject>Ran</subject><subject>γ干扰素</subject><subject>信号通路</subject><subject>免疫共沉淀</subject><subject>异源二聚体</subject><subject>相互作用</subject><subject>结合蛋白</subject><issn>1674-7305</issn><issn>1869-1889</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNpjYuA0tDCz1DW0sLBkAbLNzE10zY0NTDkYeIuLswyAwNjYwMjcnJPBPygxTyEpMy8lMy9doaAovyQ1M0_B8v2eDqC4U4Dv-z2dYNliBU83P91zu4MMFYDyJRmpUH5xZnpeYg5Yb2JJRnliJQ8Da1piTnEqL5TmZlBycw1x9tBNzsjPSy8EqowvKMrMTSyqjDczNzY0MrUwNDcmShEADmRBmA</recordid><startdate>2017</startdate><enddate>2017</enddate><creator>Junwen Zhang XiaojieCong Jiajie Zhaoqiao Xia Yang Meng Li Hong Chen Ruifang Mi Guishan Jin Fusheng Liu Bing-Ren Huang</creator><scope>2RA</scope><scope>92L</scope><scope>CQIGP</scope><scope>~WA</scope></search><sort><creationdate>2017</creationdate><title>Ran binding protein 9(RanBPM) binds IFN-λR1 in the IFN-λsignaling 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IFN-λR1.The interaction between RanBPM and IFN-λRl was identified with a glutathione S-transferase pull-down assay and coimmunoprecipitation experiments.IFN-λ1 stimulates this interaction and affects the cellular distribution of RanBPM.However,the interaction between RanBPM and IFN-λR1 does not correlate with their conserved TRAF6-binding sites.Furthermore,we also found that RanBPM is a scaffolding protein with a modulatory function that regulates the activities of IFN-stimulated response elements.Therefore,RanBPM plays a novel role in the IFN-λ-regulated signaling pathway.</abstract></addata></record> |
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ispartof | 中国科学:生命科学英文版, 2017, Vol.60 (9), p.1030-1039 |
issn | 1674-7305 1869-1889 |
language | eng |
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source | Springer Nature |
subjects | IFN-γ Ran γ干扰素 信号通路 免疫共沉淀 异源二聚体 相互作用 结合蛋白 |
title | Ran binding protein 9(RanBPM) binds IFN-λR1 in the IFN-λsignaling pathway |
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