Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

In the inner mitochondrial membrane, several potassium channels that play a role in cell life and death have been identified. One of these channels is the ATP-regulated potassium channel (mitoK). The ROMK2 potassium channel is a potential molecular component of the mitoK channel. The current study aimed to investigate the pharmacological modulation of the activity of the ROMK2 potassium channel expressed in bacteria. ROMK2 was solubilized in polymer nanodiscs and incorporated in planar lipid bilayers. The impact of known mitoK channel modulators on the activity of the ROMK2 was characterized. We found that the ROMK2 channel was activated by the mitoK channel opener diazoxide and blocked by mitoK inhibitors such as ATP/Mg, 5-hydroxydecanoic acid, and antidiabetic sulfonylurea glibenclamide. These results indicate that the ROMK2 potassium protein may be a pore-forming subunit of mitoK and that the impact of channel modulators is not related to the presence of accessory proteins.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10052516PMC
http://dx.doi.org/10.3390/membranes13030360DOI Listing

Publication Analysis

Top Keywords

romk2 potassium
16
potassium channel
16
mitok channel
12
channel
9
channel expressed
8
expressed bacteria
8
planar lipid
8
lipid bilayers
8
activity romk2
8
channel modulators
8

Similar Publications

Mitochondrial ATP-sensitive K+ channels are closely linked to cardioprotection and are potential therapeutic targets during ischemia reperfusion (IR) injury. The renal outer medullary K+ channel isoform 2 (ROMK2) is an ATP-sensitive K+ channel found in the mitochondria of cardiomyocytes. While the germline knockout of ROMK does not mediate myocardial IR injury, the effect of ROMK loss of function on IR injury in the adult myocardium is unknown.

View Article and Find Full Text PDF
Article Synopsis
  • The study explores how mitochondrial potassium channels and the peptide Gramicidin affect ion transport and electrical properties in lipid membranes attached to gold electrodes.
  • Techniques like chronoamperometry and impedance spectroscopy were used to analyze how the potassium channel's transport abilities can be altered using the ATP-Mg complex inhibitor, and how Gramicidin's function changes when sodium replaces potassium.
  • The findings show two different current-time responses, which reflect ion movement and changes in the lipid membrane, and were further validated through experiments with self-assembled monolayers on gold surfaces.
View Article and Find Full Text PDF

In this study, we utilized enzyme-catalyzed proximity labeling with the engineered promiscuous biotin ligase Turbo-ID to identify the proxisome of the ROMK2 channel. This channel resides in various cellular membrane compartments of the cell including the plasma membrane, endoplasmic reticulum and mitochondria. Within mitochondria, ROMK2 has been suggested as a pore-forming subunit of mitochondrial ATP-regulated potassium channel (mitoK).

View Article and Find Full Text PDF

In the inner mitochondrial membrane, several potassium channels that play a role in cell life and death have been identified. One of these channels is the ATP-regulated potassium channel (mitoK). The ROMK2 potassium channel is a potential molecular component of the mitoK channel.

View Article and Find Full Text PDF

The renal-outer-medullary‑potassium (ROMK2) channel modulates potassium transport in the kidney. It has been postulated that the ROMK2 is the pore-forming subunit of the mitochondrial ATP-sensitive potassium channel as a mediator of cardioprotection. In this study, cell-free synthesis of the ROMK2 was performed in presence of membrane scaffold protein (MSP1D1) nanodiscs.

View Article and Find Full Text PDF