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

Y Yuhua Tian (Department of Biomedical Sciences, School of Veterinary Medicine, University of Pennsylvania) S Soohyeon Bae (Department of Brain Sciences, Daegu Gyeongbuk Institute of Science and Technology (DGIST)) X Xuesong Wu (Department of Chemistry and Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, iChEM) K Kyle C. Rouen (Department of Physiology and Membrane Biology, School of Medicine, University of California) A Adriana Hernández-González (Department of Physiology and Membrane Biology, University of California Davis) Y Yanxiao Han (Department of Physiology and Membrane Biology, School of Medicine, University of California) A Abdullah Al Tekreeti (Department of Physiology and Membrane Biology, School of Medicine, University of California) S Simon Vu (Department of Physiology and Membrane Biology, School of Medicine, University of California) I Irene Chen (Department of Molecular and Cell Biology, University of California) E Ellen Li (Carlmont High School) I Igor Vorobyov (Department of Physiology and Membrane Biology, School of Medicine, University of California) V Vladimir Yarov-Yarovoy (Department of Physiology and Membrane Biology, University of California Davis) B Byung-Chang Suh (Department of Brain Sciences, Daegu Gyeongbuk Institute of Science and Technology) S Samuel T. Hwang (Department of Dermatology, University of California Davis) J Jie Zheng (Key Laboratory of Radiation Physics and Technology, Ministry of Education, Institute of Nuclear Science and Technology)

Abstract

Temperature-sensitive transient receptor potential melastatin subfamily 4 (TRPM4) ion channels convert intracellular calcium increases into membrane depolarization, thereby linking these two powerful cellular signaling pathways in diverse physiological processes. TRPM4 mutations cause severe human hereditary cardiovascular and skin diseases; mysteriously, while these mutations are gain-of-function in nature, they affect the heart and the skin in a mutually exclusive manner. Here, we show that phosphatidylinositol 4,5-bisphosphate (PIP2) lipid is a required cofactor for TRPM4 activity by tightly regulating its calcium sensitivity. We detected two PIP2 binding sites and located the high-affinity site adjacent to the S4-S5 linker. We demonstrated that skin disease–associated TRPM4 mutations relieve the tight control of PIP2, resulting in elevated channel activity but only at the body surface temperature. In contrast, heart diseases are associated with mutations known to boost the number of channels, an effect we found to be annihilated by channel desensitization outside the body core. Indeed, dendritic cells from transgenic mice carrying a skin disease mutant exhibited elevated migration at 25-to-30°C range compared to those from normal mice, but no difference was observed at 37°C. These findings shed light on a molecular mechanism for dynamic regulation of cellular signaling in physiology and diseases.

Article Details

Volume / Issue Vol. 123, Issue 15
Published April 14, 2026
ISSN 0027-8424
Publisher National Academy of Sciences

Authors (15)

Y

Yuhua Tian

Department of Biomedical Sciences, School of Veterinary Medicine, University of Pennsylvania

S

Soohyeon Bae

Department of Brain Sciences, Daegu Gyeongbuk Institute of Science and Technology (DGIST)

X

Xuesong Wu

Department of Chemistry and Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, iChEM

K

Kyle C. Rouen

Department of Physiology and Membrane Biology, School of Medicine, University of California

A

Adriana Hernández-González

Department of Physiology and Membrane Biology, University of California Davis

Y

Yanxiao Han

Department of Physiology and Membrane Biology, School of Medicine, University of California

A

Abdullah Al Tekreeti

Department of Physiology and Membrane Biology, School of Medicine, University of California

S

Simon Vu

Department of Physiology and Membrane Biology, School of Medicine, University of California

I

Irene Chen

Department of Molecular and Cell Biology, University of California

E

Ellen Li

Carlmont High School

I

Igor Vorobyov

Department of Physiology and Membrane Biology, School of Medicine, University of California

V

Vladimir Yarov-Yarovoy

Department of Physiology and Membrane Biology, University of California Davis

B

Byung-Chang Suh

Department of Brain Sciences, Daegu Gyeongbuk Institute of Science and Technology

S

Samuel T. Hwang

Department of Dermatology, University of California Davis

J

Jie Zheng

Key Laboratory of Radiation Physics and Technology, Ministry of Education, Institute of Nuclear Science and Technology