title: CUEDC2 interacts with heat shock protein 70 and negatively regulates its chaperone activity.
abstract: Recently studies have revealed that CUEDC2, a CUE domain-containing protein, plays critical roles in many biological processes, such as cell cycle, inflammation and tumorigenesis. In this study, to further explore the function of CUEDC2, we performed affinity purification combined with mass spectrometry analysis to identify its interaction proteins, which led to the identification of heat shock protein 70 (HSP70). We confirmed the interaction between CUEDC2 and HSP70 in vivo by co-immunoprecipitation assays. Mapping experiments revealed that CUE domain was required for their binding, while the PBD and CT domains of HSP70, mediated the interaction with CUEDC2. The intracellular Luciferase refolding assay indicated that CUEDC2 could inhibit the chaperone activity of HSP70. Together, our results identify HSP70 as a novel CUEDC2 interaction protein and suggest that CUEDC2 might play important roles in regulating HSP70 mediated stress responses.
authors.affiliation: Department of Hepatobiliary Surgery and Hepatobiliary Surgical Institute, Chinese PLA General Hospital, Beijing 100853, China; State Key Laboratory of Proteomics, China National Center of Biomedical Analysis, 27 Tai-Ping Rd., Beijing 100850, China; Department of Hepatobiliary Surgery, NO.401 Hospital of Chinese PLA, Qingdao 266071, Shandong, China.
authors.forename: Lin
authors.initials: L
authors.lastname: Gong
authors.affiliation: State Key Laboratory of Proteomics, China National Center of Biomedical Analysis, 27 Tai-Ping Rd., Beijing 100850, China.
authors.forename: Chen Hui
authors.initials: CH
authors.lastname: Wang
authors.affiliation: State Key Laboratory of Proteomics, China National Center of Biomedical Analysis, 27 Tai-Ping Rd., Beijing 100850, China.
authors.forename: Yi Jiao
authors.initials: YJ
authors.lastname: Huang
authors.affiliation: State Key Laboratory of Proteomics, China National Center of Biomedical Analysis, 27 Tai-Ping Rd., Beijing 100850, China.
authors.forename: Feng
authors.initials: F
authors.lastname: Liu
authors.affiliation: State Key Laboratory of Proteomics, China National Center of Biomedical Analysis, 27 Tai-Ping Rd., Beijing 100850, China.
authors.forename: Teng
authors.initials: T
authors.lastname: Li
authors.affiliation: State Key Laboratory of Proteomics, China National Center of Biomedical Analysis, 27 Tai-Ping Rd., Beijing 100850, China.
authors.forename: Jiang
authors.initials: J
authors.lastname: Dai
authors.affiliation: State Key Laboratory of Proteomics, China National Center of Biomedical Analysis, 27 Tai-Ping Rd., Beijing 100850, China.
authors.forename: Ai Ling
authors.initials: AL
authors.lastname: Li
authors.affiliation: State Key Laboratory of Proteomics, China National Center of Biomedical Analysis, 27 Tai-Ping Rd., Beijing 100850, China.
authors.forename: Tao
authors.initials: T
authors.lastname: Zhou
authors.affiliation: State Key Laboratory of Proteomics, China National Center of Biomedical Analysis, 27 Tai-Ping Rd., Beijing 100850, China. Electronic address: qxia@ncba.ac.cn.
authors.forename: Qing
authors.initials: Q
authors.lastname: Xia
authors.affiliation: State Key Laboratory of Proteomics, China National Center of Biomedical Analysis, 27 Tai-Ping Rd., Beijing 100850, China. Electronic address: lchen@ncba.ac.cn.
authors.forename: Liang
authors.initials: L
authors.lastname: Chen
mesh_terms: D048868:Adaptor Proteins, Signal Transducing; D002352:Carrier Proteins / Q000378:metabolism* / Q000502:physiology; D057809:HEK293 Cells; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D047468:Immunoprecipitation; D008565:Membrane Proteins / Q000378:metabolism* / Q000502:physiology; D018832:Molecular Chaperones / Q000037:antagonists & inhibitors
chemical_list: D048868:Adaptor Proteins, Signal Transducing; C519556:CUEDC2 protein, human; D002352:Carrier Proteins; D018840:HSP70 Heat-Shock Proteins; D008565:Membrane Proteins; D018832:Molecular Chaperones
keywords: CUEDC2; Chaperone activity; HSP70; Protein–protein interaction