MafG controls the hypoxic response of cells by accumulating HIF-1α in the nuclei

We identified MafG as a protein that interacts with HIF-1α, a key factor in hypoxic response, using the yeast two-hybrid system. Interaction between MafG and HIF-1α was confirmed by surface plasmon resonance and by translocation to the nucleolus with the NoLS signal. A knockdown of MafG reduced erythropoietin (EPO) mRNA levels as well as luciferase reporter activity with the hypoxia response element. The knockdown of MafG did not change total HIF-1α protein, but reduced the accumulation of HIF-1α in the nuclei. These results suggest that MafG regulates the hypoxic response of cells by detaining HIF-1α in the nuclei.Structured summaryMINT-6550898:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with MAFG (uniprotkb:Q9BRP3) by two hybrid (MI:0018)MINT-6550966:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with HSP90 alpha (uniprotkb:P07900) by surface plasmon resonance (MI:0107)MINT-6550948:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with MAFK (uniprotkb:A5PLQ5) by surface plasmon resonance (MI:0107)MINT-6550925:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with MAFG (uniprotkb:Q9BRP3) by surface plasmon resonance (MI:0107)MINT-6550912:MAFG (uniprotkb:Q9BRP3) and HIF1A (uniprotkb:Q16665) physically interact (MI:0218) by fluorescence microscopy (MI:0416)MINT-6550980:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with HSP90 beta (uniprotkb:P08238) by surface plasmon resonance (MI:0107)