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Related Concept Videos

Electrochemical Gradient and Channel Proteins: An Overview01:21

Electrochemical Gradient and Channel Proteins: An Overview

An electrochemical gradient is a fundamental concept in biology and chemistry. It regulates the movement of ions across cell membranes. This movement is influenced by two factors:
The electrical gradient: The electrical gradient across cell membranes refers to the difference in electric charge between the inside and outside of a cell.  This difference drives the movement of ions towards or away from the cells. For instance, if the inside of the cell is more negatively charged relative to the...
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The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
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Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
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A postsynaptic neuron usually receives numerous impulses from several other presynaptic neurons. The axon hillock of the postsynaptic neuron integrates all these signals and determines the likelihood of firing an action potential.
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Non-gated Ion Channels01:24

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Related Experiment Video

Updated: Jun 22, 2026

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers
09:54

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers

Published on: November 19, 2015

The SecY complex forms a channel capable of ionic discrimination.

Kush Dalal1, Franck Duong

  • 1Department of Biochemistry and Molecular Biology, Life Sciences Institute, Faculty of Medicine, University of British Columbia, Vancouver, British Columbia, Canada.

EMBO Reports
|June 2, 2009
PubMed
Summary

Even with a compromised seal, the bacterial SecY channel remains selective for anions like chloride, not generally permeable. This anion selectivity is conserved and linked to protein translocation, suggesting a pore ring selectivity filter.

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Last Updated: Jun 22, 2026

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers
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Published on: November 19, 2015

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Published on: February 23, 2017

Area of Science:

  • Membrane biology
  • Protein translocation
  • Ion channel function

Background:

  • Protein transport across bacterial membranes relies on the SecY complex.
  • The SecY channel's plug domain normally prevents small molecule passage.
  • Understanding SecY channel gating and permeability is crucial for cell physiology.

Purpose of the Study:

  • To investigate the permeability and ion selectivity of the SecY channel when its plug domain is compromised.
  • To determine if imperfect plug sealing leads to general membrane permeability.
  • To explore the role of the pore ring structure in SecY channel function and selectivity.

Main Methods:

  • Analysis of SecY channel mutants with altered plug domain interactions.
  • Electrophysiological measurements to assess ionic conductance and selectivity.
  • Comparative studies of SecY complexes from bacteria and archaea.

Main Results:

  • Loosely sealed or open-locked SecY channels do not exhibit general permeability.
  • A strong selectivity for small monovalent anions, particularly chloride, is observed.
  • Mutations in the pore ring structure enhance translocation and conductance while maintaining anion selectivity.
  • Similar ionic specificity is found during protein translocation and in archaeal SecY complexes.

Conclusions:

  • The SecY channel possesses inherent anion selectivity, even with a compromised plug.
  • The pore ring structure likely acts as a selectivity filter, conserved across species.
  • This filter allows cells to tolerate SecY channels with imperfect plug sealing during protein translocation.