Decidual protein induced by progesterone enhances HIF ‐1α stability to promote mitophagy and glycolysis

Apr 1, 2026The FEBS journal

A protein triggered by progesterone helps stabilize a key cell stress factor to increase mitochondrial recycling and sugar metabolism

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Abstract

Decidual protein induced by progesterone (DEPP) significantly influences mitophagy through the DEPP-HIF-1α-BNIP3/NIX axis.

DEPP enhances the stability of hypoxia-inducible factor 1-alpha (HIF-1α), which may promote the transcription of its target genes.
The interaction between DEPP and HIF-1α is associated with increased expression of mitophagy-related genes BNIP3 and BNIP3L (NIX).
DEPP's role in stabilizing HIF-1α could also affect the transcription of genes related to cellular metabolism.
These findings suggest that DEPP may play a critical role in regulating both mitophagy and cellular energy balance.

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Mitophagy, the process of removing mitochondria through the autophagy-lysosome pathway, is crucial for maintaining cellular homeostasis. However, its regulatory mechanisms and pathological implications remain poorly understood. In our study, we revealed that decidual protein induced by progesterone (DEPP) plays a significant role in mitophagy through the DEPP-HIF-1α-BNIP3/NIX axis. Our findings indicate that interaction between DEPP and hypoxia-inducible factor 1-alpha (HIF-1α) enhances HIF-1α stability, thereby promoting the transcription of HIF-1 target genes. The enhanced protein stability of HIF-1α not only activates mitophagy by stimulating the transcription of BCL2-interacting protein 3 (BNIP3) and BCL2-interacting protein 3-like (BNIP3L; also known as NIX) mRNA but also influences cellular metabolic reprogramming by promoting the transcription of glycolysis-related genes. In conclusion, our findings suggest that DEPP may act as a potential regulator of mitophagy and HIF-1α, playing an important role in maintaining cellular metabolic and energy homeostasis.

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Decidual protein induced by progesterone enhances HIF ‐1α stability to promote mitophagy and glycolysis

Abstract

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