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April 10, 2026Proceedings of the National Academy of SciencesOpen Access

Heat- and PIP2-dependent TRPM4 activity underlies mutually exclusive human diseases

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Authors

YTYuhua TianSBSoohyeon BaeXWXuesong Wu

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Overview

Demonstrates how TRPM4 mutations affect disease outcomes in cardiovascular and skin conditions, suggesting distinct pathogenic mechanisms.

Key Points

  • The research investigates how TRPM4 mutations cause mutually exclusive diseases, focusing on temperature and PIP2 dependency.
  • Analyzed TRPM4 activity related to calcium signaling in physiological processes.
  • Examined PIP2 as a cofactor necessary for TRPM4 function and its binding sites.
  • Conducted experiments using transgenic mice to compare cellular behaviors associated with TRPM4 mutations.
  • Identified two PIP2 binding sites critical for TRPM4's calcium sensitivity.
  • Skin disease mutations increased channel activity at lower temperatures, while heart disease mutations did not affect activity at core body temperature.
  • Dendritic cells with skin disease mutations showed increased migration at 25-30°C compared to normal mice.

Cite This Study

Tian et al. (2026) studied this question.

synapsesocial.com/papers/69d893a86c1944d70ce04989https://doi.org/10.1073/pnas.2530328123
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1BPS2026 – Heat- and PIP2-dependent TRPM4 activity underlies mutually exclusive human diseases2026
  2. 2Species-Specific Regulation of TRPM2 by PI(4,5)P2 via the Membrane Interfacial Cavity2021 · 12 citations
  3. 3Domain zipping and unzipping modulates TRPM4’s properties in human cardiac conduction disease2020 · 9 citations
  4. 4Temperature and intrinsic Ca2+ reshape TRPM4 pharmacology2026
  5. 5Four TRPM4 Cation Channel Mutations Found in Cardiac Conduction Diseases Lead to Altered Protein Stability2018 · 50 citations