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Calcium interaction with Nav1.5 via FGF12A and CaM binding.

Lucy Woodbury¹, Anna Li¹, Paweorn Angsutararux²

¹Department of Biomedical Engineering, McKelvey School of Engineering, Washington University in St. Louis, St. Louis, MO, USA.

Biorxiv : the Preprint Server for Biology

|February 6, 2026

Summary

This summary is machine-generated.

Calmodulin (CaM) and fibroblast growth factor 12A (FGF12A) interact with cardiac sodium channels (Nav1.5) in a calcium-dependent manner. This interaction modulates Nav1.5 inactivation, impacting cardiac action potentials.

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Area of Science:

Cardiovascular Physiology
Molecular Biology
Ion Channel Function

Background:

Voltage-gated sodium channels (Nav) are crucial for action potential initiation.
Nav1.5 inactivation is regulated by accessory proteins like calmodulin (CaM) and fibroblast growth factors (iFGF).
The role of intracellular calcium ([Ca2+]i) in modulating Nav1.5 gating via CaM is debated.

Purpose of the Study:

To investigate the synergistic effect of CaM and iFGF12A on Nav1.5 inactivation.
To determine if this interaction is calcium-dependent.
To elucidate the stoichiometry of the Nav1.5 CTD:CaM:iFGF12A complex.

Main Methods:

Fluorescence Resonance Energy Transfer (FRET) imaging in live cells.
Observation of interactions between Nav1.5 alpha subunit, CaM, and iFGF12A.
Comparison of Nav1.5 voltage-dependent gating kinetics under varying [Ca2+]i.

Main Results:

At resting [Ca2+]i, a 2:1 FRET efficiency suggests one CaM per Nav1.5 CTD with FGF12A.
Increased [Ca2+]i leads to equalized FRET efficiencies, indicating a 2:1:1 ratio of CaM:FGF12A:Nav1.5 CTD.
Low [Ca2+]i shifts Nav1.5 steady-state inactivation towards hyperpolarization in the presence of FGF12A.

Conclusions:

The FGF12A:CaM complex modulates Nav1.5 steady-state inactivation in a calcium-dependent manner.
This calcium-dependent mechanism allows FGF12A to regulate Nav1.5 inactivation.
Biological redundancy exists to maintain Nav1.5 inactivation stability in the absence of CaM.