Molecular Determinants of Interactions between the N-Terminal Domain and the Transmembrane Core That Modulate hERG K+ Channel Gating
2011

How the N-Terminal Domain Affects hERG K+ Channel Gating

publication Evidence: moderate

Author Information

Author(s): Fernández-Trillo Jorge, Barros Francisco, Machín Angeles, Carretero Luis, Domínguez Pedro, de la Peña Pilar

Primary Institution: Department of Biochemistry and Molecular Biology, University of Oviedo, Oviedo, Spain

Hypothesis

The N-terminal domain of the hERG potassium channel is critical for its slow deactivation gating.

Conclusion

The study found that the N-terminal domain can restore normal deactivation properties in hERG channels that have been altered.

Supporting Evidence

  • The N-terminal domain can restore normal deactivation properties in hERG channels.
  • Mutations in the N-terminal domain affect the channel's ability to deactivate properly.
  • Fluorescence resonance energy transfer (FRET) showed interactions between the N-terminal domain and the channel.

Takeaway

Scientists discovered that a part of a protein called the N-terminal domain helps a heart channel work properly, even when it has been changed.

Methodology

The researchers used mammalian cell lines to express different hERG constructs and measured their deactivation kinetics using electrophysiological techniques.

Statistical Information

P-Value

p<0.02

Statistical Significance

p<0.05

Digital Object Identifier (DOI)

10.1371/journal.pone.0024674

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