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Updated: Feb 23, 2026

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes
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SUMO co-expression modifies KV 11.1 channel activity.

A B Steffensen1, M N Andersen1, N Mutsaers1

  • 1Department of Biomedical Sciences, Faculty of Health and Medical Sciences, Danish National Research Foundation Centre for Cardiac Arrhythmia, University of Copenhagen, Copenhagen, Denmark.

Acta Physiologica (Oxford, England)
|September 10, 2017
PubMed
Summary
This summary is machine-generated.

Sumoylation modifies the cardiac potassium channel KV 11.1 (also known as IKr), impacting its electrical activity. This study identifies specific sites on the channel affected by sumoylation.

Keywords:
KV11.1sumoylationtwo-electrode voltage-clamp electrophysiology

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Area of Science:

  • Molecular biology
  • Cardiovascular physiology
  • Ion channel function

Background:

  • The KV 11.1 channel (IKr) is crucial for heart rhythm.
  • Channel dysfunction causes cardiac arrhythmias.
  • Discrepancies between native and experimental currents suggest unknown regulatory factors.

Purpose of the Study:

  • To investigate the role of sumoylation in regulating KV 11.1 channel activity.
  • To identify specific sumoylation sites on the KV 11.1 channel.

Main Methods:

  • Electrophysiological recordings using two-electrode voltage-clamp (TEVC) in Xenopus oocytes.
  • Site-directed mutagenesis to pinpoint SUMO-target amino acids.
  • Confocal imaging for protein localization studies.

Main Results:

  • Sumoylation of KV 11.1 alters electrophysiological properties, decreasing current amplitude.
  • Observed effects are attributed to faster inactivation and modified deactivation kinetics.
  • Lysines at positions 21, 93, and 116 within the PAS domain were identified as potential SUMOylation targets.

Conclusions:

  • KV 11.1 is a target for sumoylation.
  • Specific residues (K21, K93, K116) are implicated in this modification.
  • Sumoylation of the PAS domain influences channel kinetics.