TWIK-1/TASK-3 heterodimeric channels contribute to the neurotensin-mediated excitation of hippocampal dentate gyrus granule cells

Exp Mol Med. 2018 Nov 12;50(11):1-13. doi: 10.1038/s12276-018-0172-4.

Abstract

Two-pore domain K+ (K2P) channels have been shown to modulate neuronal excitability. The physiological role of TWIK-1, the first identified K2P channel, in neuronal cells is largely unknown, and we reported previously that TWIK-1 contributes to the intrinsic excitability of dentate gyrus granule cells (DGGCs) in mice. In the present study, we investigated the coexpression of TWIK-1 and TASK-3, another K2P member, in DGGCs. Immunohistochemical staining data showed that TASK-3 proteins were highly localized in the proximal dendrites and soma of DGGCs, and this localization is similar to the expression pattern of TWIK-1. TWIK-1 was shown to associate with TASK-3 in DGGCs of mouse hippocampus and when both genes were overexpressed in COS-7 cells. shRNA-mediated gene silencing demonstrated that TWIK-1/TASK-3 heterodimeric channels displayed outwardly rectifying currents and contributed to the intrinsic excitability of DGGCs. Neurotensin-neurotensin receptor 1 (NT-NTSR1) signaling triggered the depolarization of DGGCs by inhibiting TWIK-1/TASK-3 heterodimeric channels, causing facilitated excitation of DGGCs. Taken together, our study clearly showed that TWIK-1/TASK-3 heterodimeric channels contribute to the intrinsic excitability of DGGCs and that their activities are regulated by NT-NTSR1 signaling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • COS Cells
  • Chlorocebus aethiops
  • Dentate Gyrus / cytology
  • Dentate Gyrus / metabolism*
  • Dentate Gyrus / physiology
  • Excitatory Postsynaptic Potentials*
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Neurons / metabolism
  • Neurons / physiology
  • Neurotensin / metabolism
  • Potassium Channels / metabolism*
  • Potassium Channels, Tandem Pore Domain / metabolism*
  • Protein Multimerization*

Substances

  • Kcnk1 protein, mouse
  • Potassium Channels
  • Potassium Channels, Tandem Pore Domain
  • TASK3 protein, mouse
  • Neurotensin