Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

6.9K
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,...
6.9K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

7.0K
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,...
7.0K
Structure of Cadherins01:25

Structure of Cadherins

5.1K
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...
5.1K
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

4.1K
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
4.1K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

9.3K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
9.3K
Catenins01:23

Catenins

3.2K
Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the...
3.2K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Barium senses subtle pore changes in a voltage-gated K<sup>+</sup> channel associated with voltage sensor states and regulatory subunits.

Science advances·2026
Same author

Differential effects of semaglutide and colchicine on atrial remodeling in rats with reduced ejection fraction after myocardial infarction.

Europace : European pacing, arrhythmias, and cardiac electrophysiology : journal of the working groups on cardiac pacing, arrhythmias, and cardiac cellular electrophysiology of the European Society of Cardiology·2026
Same author

The Concise Guide to PHARMACOLOGY 2025/26: Ion channels.

British journal of pharmacology·2025
Same author

Live-cell quantitative monitoring reveals distinct, high-affinity Gβγ regulations of GIRK2 and GIRK1/2 channels.

Nature communications·2025
Same author

Live-cell quantitative monitoring reveals distinct, high-affinity Gβγ regulations of GIRK2 and GIRK1/2 channels.

bioRxiv : the preprint server for biology·2025
Same author

Structural basis for ATP-driven double-ring assembly of the human mitochondrial Hsp60 chaperonin.

bioRxiv : the preprint server for biology·2025

Related Experiment Video

Updated: Mar 15, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

26.0K

Structural Insights into the M-Channel Proximal C-Terminus/Calmodulin Complex.

Roi Strulovich1, William Sam Tobelaim1, Bernard Attali1

  • 1Department of Biochemistry and Molecular Biology, Institute of Structural Biology, George S. Wise Faculty of Life Sciences, ‡Department of Physiology and Pharmacology, Sackler Faculty of Medicine, and §Sagol School of Neuroscience, Tel Aviv University , Ramat Aviv 69978, Israel.

Biochemistry
|August 27, 2016
PubMed
Summary

Kv7 channels, crucial for cellular excitability, feature a calmodulin-binding C-terminal domain. Structural analysis of Kv7.3 helix A and Kv7.2 helix B interactions reveals insights into M channel function and stabilization.

More Related Videos

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
13:40

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

Published on: July 7, 2011

18.7K
In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
10:05

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

11.8K

Related Experiment Videos

Last Updated: Mar 15, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

26.0K
Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
13:40

Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms

Published on: July 7, 2011

18.7K
In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes
10:05

In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

Published on: August 13, 2012

11.8K

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biophysics

Background:

  • Kv7 (KCNQ) channels are voltage-gated potassium channels vital for regulating neuronal excitability.
  • Their intracellular C-terminal (CT) domain, constitutively bound by calmodulin (CaM), is essential for channel assembly and function.
  • Kv7.2 and Kv7.3 subunits form the heterotetrameric M channel, critical in neural tissues.

Purpose of the Study:

  • To characterize the Kv7.2, Kv7.3, and chimeric CT/CaM complexes.
  • To determine the structural basis of CaM interaction with Kv7 channel CT domains.
  • To elucidate the role of specific helices in Kv7 channel assembly and gating.

Main Methods:

  • Solution-based biophysical methods to study CT/CaM complexes.
  • X-ray crystallography to determine high-resolution structures.
  • Functional characterization of chimeric channels.

Main Results:

  • Kv7.2, Kv7.3, and chimeric CT/CaM complexes exhibit 1:1 stoichiometry.
  • Crystal structure of the chimeric Q3A-Q2B/CaM complex reveals CaM interaction with helices A and B.
  • The structure shows unique interactions and a hybrid CaM conformation, highlighting Kv7.3 helix A's role in stabilization and oligomerization.

Conclusions:

  • Kv7.3 helix A is crucial for stabilizing Kv7 channel oligomerization.
  • The determined structure provides a basis for understanding channelopathies.
  • The chimeric channel's gating properties underscore helix A's importance in imparting channel function.