CUEDC2 interacts with heat shock protein 70 and negatively regulates its chaperone activity.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.
CUEDC2
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.
HSP70