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Related Concept Videos

Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...
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...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

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...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

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...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

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[Conserved motifs in voltage sensing proteins].

Chang-He Wang1, Zhen-Li Xie, Jian-Wei Lv

  • 1College of Life Science, Agriculture and Forestry, Qiqihar University, Qiqihar 161006, China. changhecool@163.com

Sheng Li Xue Bao : [Acta Physiologica Sinica]
|August 22, 2012
PubMed
Summary

Voltage sensing proteins (VSPs) share conserved motifs crucial for detecting membrane potential. Key findings reveal specific charged residues in transmembrane segments S3 and S4 are vital for voltage sensing mechanisms.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Voltage-sensing proteins (VSPs) are critical for cellular electrical signaling.
  • Understanding VSPs' conserved motifs is essential for modeling their function.
  • Known VSPs include voltage-gated ion channels and voltage-dependent phosphatases.

Purpose of the Study:

  • To investigate conserved motifs within voltage-sensing proteins (VSPs).
  • To develop a functional model for voltage sensing mechanisms.
  • To identify the significance of conserved residues in VSP transmembrane segments.

Main Methods:

  • Data collection from the UniProt database via keyword search and manual curation.
  • Profile-to-profile sequence alignments to identify conserved motifs and residues.
  • Analysis of four-helix transmembrane segments (S1-S4) common to all VSPs.

Main Results:

  • Identified two primary types of VSPs: voltage-gated ion channels and voltage-dependent phosphatases.
  • All VSPs possess a conserved four-helical transmembrane segment (S1-S4) voltage-sensing module.
  • A highly conserved motif ([RK]-X(2)-R-X(2)-R-X(2)-[RK]) in S4 and a conserved aspartate in S3 were identified as critical for voltage sensing.

Conclusions:

  • Conserved motifs across VSPs, particularly in S3 and S4, are fundamental to their voltage-sensing capabilities.
  • The movement of charged residues in S4 and interactions with S3 are key to detecting membrane potential changes.
  • These findings enhance our understanding of VSP structure-function relationships and provide a basis for voltage-sensing models.