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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Gong L,Wang CH,Huang YJ,Liu F,Li T,Dai J,Li AL,Zhou T,Xia Q,Chen Ldoi
10.1016/j.bbrc.2014.03.102subject
Has Abstractpub_date
2014-04-25 00:00:00pages
64-9issue
1eissn
0006-291Xissn
1090-2104pii
S0006-291X(14)00554-3journal_volume
447pub_type
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