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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...

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Related Experiment Video

Updated: Jun 10, 2026

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

BK channel activation: structural and functional insights.

Urvi S Lee1, Jianmin Cui

  • 1Department of Biomedical Engineering and Cardiac Bioelectricity and Arrhythmia Center, Washington University, St. Louis, MO 63130, USA.

Trends in Neurosciences
|July 29, 2010
PubMed
Summary
This summary is machine-generated.

Voltage- and calcium-activated potassium (BK) channels regulate neuronal activity. New structural studies reveal how BK channel domains interact, advancing our understanding of channel gating and its role in epilepsy.

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Last Updated: Jun 10, 2026

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Structural Biology

Background:

  • Voltage- and Ca(2+)-activated K(+) (BK) channels are crucial for regulating neurotransmitter release and neuronal excitability.
  • BK channels share structural homology with other voltage- and ligand-gated K(+) channels, featuring distinct membrane-spanning and cytosolic domains.

Purpose of the Study:

  • To review recent structural findings on BK channel assembly and gating mechanisms.
  • To discuss the implications of these findings for understanding BK channel function in health and disease.

Main Methods:

  • Electron cryomicroscopy (cryo-EM) and X-ray crystallography were used to determine BK channel structures.
  • Functional studies have previously suggested close interactions between BK channel domains during gating.

Main Results:

  • Recent structural studies provide unprecedented insights into the assembly of BK channel domains.
  • These structures corroborate functional data, highlighting domain interactions critical for channel gating.

Conclusions:

  • Emerging structural data are reshaping our understanding of BK channel gating mechanisms.
  • Understanding BK channel gating is vital for investigating diseases like epilepsy, linked to mutations in BK channel genes.