Direct manipulation of a single potassium channel gate with an atomic force microscope probe

Mitsunori Kitta, Toru Ide, Minako Hirano, Hiroyuki Tanaka, Toshio Yanagida, Tomoji Kawai

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Ion channels are membrane proteins that regulate cell functions by controlling the ion permeability of cell membranes. An ion channel contains an ion-selective pore that permeates ions and a sensor that senses a specific stimulus such as ligand binding to regulate the permeability. The detailed molecular mechanisms of this regulation, or gating, are unknown. Gating is thought to occur from conformational changes in the sensor domain in response to the stimulus, which results in opening the gate to permit ion conduction. Using an atomic force microscope and artificial bilayer system, a mechanical stimulus is applied to a potassium channel, and its gating is monitored in real time. The channel-open probability increases greatly when pushing the cytoplasmic domain toward the membrane. This result shows that a mechanical stimulus at the cytoplasmic domain causes changes in the gating and is the first to show direct evidence of coupling between conformational changes in the cytoplasmic domain and channel gating. This novel technology has the potential to be a powerful tool for investigating the activation dynamics in channel proteins. An atomic force microscope is used to apply a mechanical stimulus to a potassium channel protein, and its gating is monitored in real time. The channel-open probability increases greatly when pushing the cytoplasmic domain toward the membrane. This provides direct evidence of coupling between conformational changes in the cytoplasmic domain and channel gating.

Original languageEnglish
Pages (from-to)2379-2383
Number of pages5
JournalSmall
Volume7
Issue number16
DOIs
Publication statusPublished - Aug 22 2011
Externally publishedYes

Fingerprint

Potassium Channels
Potassium
Microscopes
Ions
Ion Channels
Cell Membrane Permeability
Proteins
Membranes
Sensors
Cell membranes
Permeability
Membrane Proteins
Chemical activation
Ligands
Technology

Keywords

  • atomic force microscopy
  • gating
  • ion channels
  • protein structures
  • single-molecule studies

ASJC Scopus subject areas

  • Biomaterials
  • Engineering (miscellaneous)
  • Biotechnology
  • Medicine(all)

Cite this

Direct manipulation of a single potassium channel gate with an atomic force microscope probe. / Kitta, Mitsunori; Ide, Toru; Hirano, Minako; Tanaka, Hiroyuki; Yanagida, Toshio; Kawai, Tomoji.

In: Small, Vol. 7, No. 16, 22.08.2011, p. 2379-2383.

Research output: Contribution to journalArticle

Kitta, M, Ide, T, Hirano, M, Tanaka, H, Yanagida, T & Kawai, T 2011, 'Direct manipulation of a single potassium channel gate with an atomic force microscope probe', Small, vol. 7, no. 16, pp. 2379-2383. https://doi.org/10.1002/smll.201002337
Kitta, Mitsunori ; Ide, Toru ; Hirano, Minako ; Tanaka, Hiroyuki ; Yanagida, Toshio ; Kawai, Tomoji. / Direct manipulation of a single potassium channel gate with an atomic force microscope probe. In: Small. 2011 ; Vol. 7, No. 16. pp. 2379-2383.
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