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SUMOylation of the Cardiac Sodium Channel NaV1.5 Modifies Inward Current and Cardiac Excitability
Journal article   Peer reviewed

SUMOylation of the Cardiac Sodium Channel NaV1.5 Modifies Inward Current and Cardiac Excitability

Jin-Young Yoon, Alexander M Greiner, Julia S Jacobs, Young-Rae Kim, Tyler P Rasmussen, William J Kutschke, Daniel S Matasic, Ajit Vikram, Ravinder R Gaddam, Haider Mehdi, …
Heart rhythm, Vol.20(11), pp.1548-1557
10/31/2023
DOI: 10.1016/j.hrthm.2023.07.067
PMCID: PMC12007604
PMID: 37543305

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Abstract

Background Decreased peak sodium current (I Na ) and increased late sodium current (I Na,L ), through the cardiac sodium channel Na V 1.5 encoded by SCN5A , cause arrhythmias. Many Na V 1.5 post-translational modifications have been reported. A recent report concluded that acute hypoxia increases I Na,L by increasing a Small Ubiquitin-like MOdifier (SUMOylation) at K442-Na V 1.5. Objective To determine whether and by what mechanisms SUMOylation alters I Na , I Na,L and cardiac electrophysiology. Methods SUMOylation of Na V 1.5 was detected by immunoprecipitation and immunoblotting. I Na was measured by patch clamp with/without SUMO1 overexpression in HEK293 cells expressing wild type (WT) or K442R-Na V 1.5 and in neonatal rat cardiac myocytes (NRCMs). SUMOylation effects were studied in vivo by electrocardiograms and ambulatory telemetry using Scn5a heterozygous knockout (SCN5A +/- ) mice and the de-SUMOylating protein SENP2 (AAV9-SENP2), AAV9-SUMO1, or the SUMOylation inhibitor anacardic acid. Na V 1.5 trafficking was detected by immunofluorescence. Results Na V 1.5 was SUMOylated in HEK293 cells, NRCMs and human heart tissue. HyperSUMOylation at Na V 1.5-K442 increased I Na in NRCMs and in HEK cells overexpressing WT but not K442R-Na v 1.5. SUMOylation did not alter other channel properties including I Na,L . AAV9-SENP2 or anacardic acid decreased I Na , prolonged QRS duration, and produced heart block and arrhythmias in SCN5A +/- mice, while AAV9-SUMO1 increased I Na and shortened QRS duration . SUMO1 overexpression enhanced membrane localization of Na V 1.5. Conclusion SUMOylation of K442-Na v 1.5 increases peak I Na without changing I Na,L , at least in part by altering membrane abundance. Our findings do not support SUMOylation as a mechanism for changes in I Na,L. Na v 1.5 SUMOylation may modify arrhythmic risk in disease states and represents a potential target for pharmacological manipulation.

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