MinK channels

A minimal channel protein with a maximal impact

Andreas E. Busch, James Maylie

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

MinK channels represent a family of voltage-gated potassium channels with a very distinct molecular structure and unique kinetic properties. The minK channel subunit contains only one transmembrane-spanning region, but the mechanism of channel formation remains unclear. There is some indication that assembly of the subunits plays a role in channel activation which may also explain the very slow activation kinetics of minK channels. MinK channels are regulated by a number of second messengers such as [Ca2+]i, cyclic-AMP and diacylglycerol also known to modulate cell excitability. This regulation indicates the putative role of minK channels in the modulation of cell excitability in the tissues where they are expressed. In cardiac myocytes, the potassium conductance IKs displays similar properties to minK channels expressed in Xenopus oocytes. As this conductance plays a crucial role for the induction of action potential repolarization, it could be a very important target for agents meant to suppress heart rhythm disturbances. Clarification of the minK channel structure and the physiological significance of this channel remains a very important goal.

Original languageEnglish (US)
Pages (from-to)270-276
Number of pages7
JournalCellular Physiology and Biochemistry
Volume3
Issue number5-6
DOIs
StatePublished - 1993

Fingerprint

Mink
Proteins
Voltage-Gated Potassium Channels
Diglycerides
Second Messenger Systems
Xenopus
Molecular Structure
Cardiac Myocytes
Cyclic AMP
Action Potentials
Oocytes
Potassium

Keywords

  • Heart
  • Kidney
  • Potassium channel
  • Regulation

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Cite this

MinK channels : A minimal channel protein with a maximal impact. / Busch, Andreas E.; Maylie, James.

In: Cellular Physiology and Biochemistry, Vol. 3, No. 5-6, 1993, p. 270-276.

Research output: Contribution to journalArticle

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