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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...
The Role of Ion Channels in Neuronal Computation01:19

The Role of Ion Channels in Neuronal Computation

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.
Sometimes a single EPSP is strong enough to induce an action potential in the postsynaptic neuron. However, multiple presynaptic inputs must often create EPSPs around the same time for the postsynaptic neuron to be sufficiently depolarized to fire an action potential.
Gap Junctions01:27

Gap Junctions

The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...
Gap Junctions01:37

Gap Junctions

Multicellular organisms employ a variety of ways for cells to communicate with each other. Gap junctions are specialized proteins that form pores between neighboring cells in animals, connecting the cytoplasm between the two, and allowing for the exchange of molecules and ions. They are found in a wide range of invertebrate and vertebrate species, mediate numerous functions including cell differentiation and development, and are associated with numerous human diseases, including cardiac and...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...

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Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
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Structure-function relationships of the NCKX2 Na+/Ca2+-K+ exchanger.

Y Shibukawa1, K J Kang, T G Kinjo

  • 1Department of Physiology and Biophysics, Faculty of Medicine, University of Calgary, 3330 Hospital Drive, N.W. Calgary, Alberta, T2N 4N1, Canada.

Annals of the New York Academy of Sciences
|February 17, 2007
PubMed
Summary

K+-dependent Na+/Ca2+ exchangers (NCKX) are vital for many bodily functions. This review details NCKX2 structure and key residues for cation transport and binding.

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Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane
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Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

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Recapitulation of an Ion Channel IV Curve Using Frequency Components
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Recapitulation of an Ion Channel IV Curve Using Frequency Components

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Last Updated: Jul 16, 2026

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
10:19

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes

Published on: January 10, 2011

Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane
07:38

Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Published on: March 30, 2015

Recapitulation of an Ion Channel IV Curve Using Frequency Components
10:14

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Published on: February 8, 2011

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • K+-dependent Na+/Ca2+ exchangers (NCKX) are crucial for diverse physiological processes.
  • These include phototransduction, motor learning, memory, and skin pigmentation.
  • NCKX proteins belong to the human SLC24 gene family, with isoforms NCKX1-5.

Purpose of the Study:

  • To review recent findings on the NCKX2 protein.
  • To elucidate the topological arrangement of its transmembrane segments involved in cation transport.
  • To identify residues critical for NCKX2 transport function and cation binding.

Main Methods:

  • Structure-function analysis of the NCKX2 protein.
  • Sequence similarity comparisons across NCKX isoforms (NCKX1-5).

Main Results:

  • Detailed review of NCKX2 transmembrane segment organization.
  • Identification of specific residues essential for cation transport and binding.
  • Extrapolation of NCKX2 findings to other NCKX isoforms based on sequence homology.

Conclusions:

  • NCKX2 structure and function provide insights applicable to the broader SLC24 gene family.
  • Understanding NCKX topology and key residues is vital for comprehending their physiological roles.
  • This review consolidates knowledge on NCKX protein mechanisms.