Insulin receptor substrate 4 deficiency mediates the insulin effect on the epithelial magnesium channel TRPM6 and causes hypomagnesemia
J. Zhang, S. W. An, S. Neelam, A. Bhatta, M. Nie, C. Duran, M. Bal, F. Latta, J. S. Hou, J. J. Otto, J. Kozlitina, A. Lemoff, J. Hoenderop, M. Baum, M. T. Wolf
Abstract
The kidney is the key regulator of magnesium (Mg2+) homeostasis in the human body. In the distal convoluted tubule (DCT), the apical epithelial magnesium (Mg2+) channel TRPM6, determines how much Mg2+ is excreted in the urine. To better understand the regulation of human renal Mg2+ absorption we identified novel, potential interaction partners of TRPM6 by pursuing a liquid chromatography - tandem mass spectrometry (LC-MS/MS) proteomics approach. We found insulin receptor substrate 4 (IRS4) enriched with TRPM6 tagged to glutathione S-transferase (TRPM6-GST) but not GST control. Physical interaction between IRS4 and TRPM6 was confirmed by co-immunoprecipitation. Applying microdissection of mouse tubules, we detected Irs4 mRNA expression mostly in the DCT and to a lower degree in the proximal tubule and thick ascending limb of Henle. Given the overall low abundance of Irs4 mRNA along the tubule we investigated the phenotype of Irs4 knockout mice (Irs4-/-). These Irs4-/- mice displayed significantly higher urinary and fecal Mg2+ losses and lower blood Mg2+ levels than wild-type (WT) mice. Claudin-16, claudin-19, and Hnf1b mRNA and Claudin-16 and Trpm6 protein expression was significantly higher in kidneys of 3 month old Irs4-/- mice consistent with a compensatory mechanism to conserve Mg2+. Applying whole-cell patch-clamp recording we confirmed the stimulatory role of insulin on TRPM6 channel activity and showed that IRS4 targets the two TRPM6 phosphorylation sites T1391 and S1583 to enhance TRPM6 current density. To test the effect of Mg2+ deficiency on metabolism, we performed glucose and insulin tolerance studies, which were mildly abnormal in Irs4-/- mice. SIGNIFICANCE STATEMENTMagnesium (Mg2+) is the second most abundant intracellular cation but the regulation of Mg2+ homeostasis is not well understood. The kidney is the key organ for regulating Mg2+ homeostasis. Insulin is a known stimulator of the apical epithelial Mg2+channel TRPM6. We present a novel modifier of Mg2+ absorption with insulin receptor substrate 4 (IRS4) which illuminates further, how insulin activates the TRPM6 channel and modifies Mg2+ homeostasis. Applying protein biochemistry, tubular microdissection, whole mouse physiology, and patch-clamp recording, we demonstrate that IRS4 mediates the stimulatory effect of insulin by enhancing phosphorylation of two specific TRPM6 residues. Irs4-/- mice develop increased urinary and stool Mg2+ losses, lower serum Mg2+ concentration, and display mild impairment in glucose and insulin tolerance.
02 /Specification & Classification
Click any tag to browse matching papers- Organism
- Assay
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- MG53 is not a critical regulator of insulin signaling pathway in skeletal muscle
P. Delerive, C. Philouze, … N. Provost·bioRxiv·Dec 24, 2020
- Insulin promoted mobilization of GLUT4 from a perinuclear storage site requires RAB10.
A. Brumfield, N. Chaudhary, … T. E. McGraw·bioRxiv·Apr 14, 2020
- Coordinated Regulation of Renal Glucose Reabsorption and Gluconeogenesis by mTORC2 and Potassium
John Eric Demko, Bidisha Saha, … David Pearce·Journal of the American Society of NephrologyPeer-reviewed·Apr 10, 2025
- Trafficking regulator of GLUT4-1 (TRARG1) is a GSK3 substrate
X. Duan, D. M. Norris, … D. J. Fazakerley·bioRxiv·Dec 7, 2020
- High-fat diet ablates an insulin-responsive pool of GLUT4 glucose transporters in skeletal muscle
Youjia Hu, Stacey N. Brown, … Jonathan S. Bogan·bioRxiv·Jun 29, 2025
- The isoforms of pyruvate kinase act as nutrient sensors for the β-cell KATP channel
H. R. Foster, T. Ho, … M. J. Merrins·bioRxiv·Feb 9, 2022