Activation gating in HCN2 channels

PLoS Comput Biol. 2018 Mar 22;14(3):e1006045. doi: 10.1371/journal.pcbi.1006045. eCollection 2018 Mar.

Abstract

Hyperpolarization-activated cyclic nucleotide-modulated (HCN) channels control electrical rhythmicity in specialized brain and heart cells. We quantitatively analysed voltage-dependent activation of homotetrameric HCN2 channels and its modulation by the second messenger cAMP using global fits of hidden Markovian models to complex experimental data. We show that voltage-dependent activation is essentially governed by two separable voltage-dependent steps followed by voltage-independent opening of the pore. According to this model analysis, the binding of cAMP to the channels exerts multiple effects on the voltage-dependent gating: It stabilizes the open pore, reduces the total gating charge from ~8 to ~5, makes an additional closed state outside the activation pathway accessible and strongly accelerates the ON-gating but not the OFF-gating. Furthermore, the open channel has a much slower computed OFF-gating current than the closed channel, in both the absence and presence of cAMP. Together, these results provide detailed new insight into the voltage- and cAMP-induced activation gating of HCN channels.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cyclic AMP / metabolism
  • Cyclic Nucleotide-Gated Cation Channels / metabolism
  • Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels / metabolism
  • Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels / physiology*
  • Ion Channel Gating / physiology*
  • Kinetics
  • Markov Chains
  • Models, Neurological
  • Oocytes / physiology
  • Patch-Clamp Techniques
  • Potassium Channels / physiology
  • Xenopus laevis / physiology

Substances

  • Cyclic Nucleotide-Gated Cation Channels
  • Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels
  • Potassium Channels
  • Cyclic AMP

Grants and funding

This work was supported by the grants BE1250/16-2, the SFB/TR 166 (Project A5) ReceptorLight and the Research Unit 2518 DynIon (Project P2) of the Deutsche Forschungsgemeinschaft to KB. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.