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PRDM 14 is overexpressed in various cancers and can regulate cancer phenotype under certain conditions. Inhibiting  PRDM 14 expression in breast and pancreatic cancers has been reported to reduce cancer stem‐like phenotypes, which are associated with aggressive tumor properties. Therefore,  PRDM 14 is considered a promising target for cancer therapy. To develop a pharmaceutical treatment, the mechanism and interacting partners of  PRDM 14 need to be clarified. Here, we identified the proteins interacting with  PRDM 14 in triple‐negative breast cancer ( TNBC ) cells, which do not express the three most common types of receptor (estrogen receptors, progesterone receptors, and  HER 2). We obtained 13 candidates that were pulled down with  PRDM 14 in  TNBC HCC 1937 cells and identified them by mass spectrometry. Two candidates—glucose‐regulated protein 78 ( GRP 78) and heat shock protein 90‐α ( HSP 90α)—were confirmed in immunoprecipitation assay in two  TNBC  cell lines ( HCC 1937 and  MDA ‐ MB 231). Surface plasmon resonance analysis using  GST ‐ PRDM 14 showed that these two proteins directly interacted with  PRDM 14 and that the interactions required the C‐terminal region of  PRDM 14, which includes zinc finger motifs. We also confirmed the interactions in living cells by NanoLuc luciferase‐based bioluminescence resonance energy transfer (Nano BRET ) assay. Moreover,  HSP 90 inhibitors (17 DMAG  and  HSP 990) significantly decreased breast cancer stem‐like  CD 24 −   CD 44 +  and side population ( SP ) cells in  HCC 1937 cells, but not in  PRDM 14 knockdown  HCC 1937 cells. The combination of the  GRP 78 inhibitor  HA 15 and  PRDM 14 knockdown significantly decreased cell proliferation and  SP  cell number in  HCC 1937 cells. These results suggest that  HSP 90α and  GRP 78 interact with  PRDM 14 and participate in cancer regulation.

PRDM14 directly interacts with heat shock proteins HSP90α and glucose‐regulated protein 78