BPGM shapes NFAT5-driven cellular responses

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Authors: Kameliya Roegner, Vera A. Kulow, Ralf Mrowka, Kristina Engel, Bayram Edemir, Mumtaz Kasim, Cem Erdogan, Laetitia Malotka, Michael Fähling, Robert Labes
Cited by: 1
References: 61

Abstract

Osmotic stress represents a major challenge to cells, particularly in the kidney, where tonicity gradients are both physiologically relevant and pathologically altered. The transcription factor nuclear factor of activated T cells 5 (NFAT5) is a key regulator of the osmoadaptive response, yet its downstream metabolic effectors remain incompletely understood. In this study, we identify the glycolytic side-branch enzyme 2,3-bisphosphoglycerate mutase (BPGM) as a transcriptional NFAT5 target that is induced under hypertonic conditions. RNA-seq analysis revealed that Bpgm knockdown significantly alters gene expression under osmotic stress (450 mOsmol/kg), with substantial overlap between BPGM- and NFAT5-responsive transcriptional programs. Bpgm depletion impairs the induction of canonical NFAT5 target genes, suggesting a functional interplay between metabolic and transcriptional adaptation. Promoter enrichment analysis showed that genes regulated by both NFAT5 and BPGM under hypertonic conditions are associated with CpG islands and GC-rich elements, supporting a link to chromatin structure and transcriptional accessibility. Consistently, we show that HIF-1α expression is regulated downstream of NFAT5 and BPGM, indicating a hierarchical organization of osmotic and hypoxic stress responses. We propose that BPGM facilitates NFAT5 function through metabolic-epigenetic coupling, acting as an amplifier of protective gene expression. Notably, this axis is active in BPGM-expressing cells such as those of the distal convoluted tubule. Thus, our findings establish BPGM as a critical node in the osmoadaptive gene regulatory network and highlight how cell type-specific metabolic profiles influence the transcriptional response to hypertonic stress.

Fields of Study & Subjects

Signaling Pathways in Disease Aldose Reductase and Taurine Nuclear Receptors and Signaling

Publication details

Journal / source
Cellular and Molecular Life Sciences
Publisher
Springer Science and Business Media LLC
Volume
83
Issue
1
Publication date
25 February 2026
Language
EN