机构地区:[1]National Laboratory of Medical Molecular Biology, Department of Biochemistry and Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing 100005, China [2]Brain Tumor Research Center, Beijing Neurosurgical Institute, Beijing Tiantan Hospital Affiliated to Capital Medical University, Beijing 100050, China [3]Beijing Laboratory of Biomedical Materials, Beijing 100050, China
出 处:《Science China(Life Sciences)》2017年第9期1030-1039,共10页中国科学(生命科学英文版)
基 金:supported by the National Natural Science Foundation of China(81302186,81372354,81672478);the Beijing Natural Science Foundation(7151002);the Beijing Laboratory of Biomedical Materials Foundation,the Beijing Neurosurgical Institute Youth Programme(2014003,2016003);the Beijing Municipal Administration of Hospitals' Youth Programme(QML20150505)
摘 要: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.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.
关 键 词:IFN-λ IFN-λR1 INTERACTION RANBPM
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...
正在载入数据...