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

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,...
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...
Catenins01:23

Catenins

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 adherens...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...

You might also read

Related Articles

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

Sort by
Same author

Saxiphilin is a broad-spectrum toxin sponge for C13-modified saxitoxins.

Structure (London, England : 1993)·2026
Same author

Structural evidence that a lipid plug controls K<sub>2P</sub>6.1(TWIK-2) function.

Nature communications·2026
Same author

Saxiphilin is a broad-spectrum toxin sponge for C13-modified saxitoxins.

bioRxiv : the preprint server for biology·2026
Same author

Saxiphilin functions as a 'toxin sponge' protein that counteracts the effects of saxitoxin poisoning.

bioRxiv : the preprint server for biology·2025
Same author

Reversible Antagonism of Dopamine D1 Receptor Using a Photoswitchable Remotely Tethered Ligand.

ACS chemical biology·2025
Same author

Deficiency in transmitter release triggers homeostatic transcriptional changes that increase presynaptic excitability.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same journal

Scalable phosphotyrosine enrichment with SH2 superbinder enables deep profiling of EGF responses.

The EMBO journal·2026
Same journal

Essential nucleus-apical pole linkage maintains division fidelity during Plasmodium progeny formation.

The EMBO journal·2026
Same journal

From cell atlases to mechanisms: bridging scRNA-seq discovery with in vivo genetics.

The EMBO journal·2026
Same journal

Mitochondrial calcium regulates lipid metabolism by modulating tethering of mitochondria to lipid droplets.

The EMBO journal·2026
Same journal

Chromosome condensation mechanically primes the nucleus for mitosis.

The EMBO journal·2026
Same journal

NDR kinase SAX-1 controls dendrite branch-specific elimination during neuronal remodeling in C. elegans.

The EMBO journal·2026
See all related articles

Related Experiment Video

Updated: Jun 8, 2026

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

Multiple C-terminal tail Ca(2+)/CaMs regulate Ca(V)1.2 function but do not mediate channel dimerization.

Eun Young Kim1, Christine H Rumpf, Filip Van Petegem

  • 1Cardiovascular Research Institute, University of California, San Francisco, CA 94158-2330, USA.

The EMBO Journal
|October 19, 2010
PubMed
Summary
This summary is machine-generated.

Two calcium ions bound to calmodulin (CaM) can simultaneously interact with the voltage-gated calcium channel Ca(V)1.2 C-terminal tail, influencing its function. This interaction, particularly at the PreIQ C-region, plays a role in calcium-dependent facilitation.

More Related Videos

Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators
11:33

Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators

Published on: March 22, 2019

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Related Experiment Videos

Last Updated: Jun 8, 2026

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

Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators
11:33

Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators

Published on: March 22, 2019

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Area of Science:

  • Molecular and Cellular Biology
  • Structural Biology
  • Biophysics

Background:

  • Voltage-gated calcium channels (Ca(V)s) are crucial for cellular signaling.
  • Calmodulin (CaM) is a key calcium-binding protein that modulates Ca(V) function.
  • Previous studies suggested Ca(V)s form dimers, but their interaction with CaM remained unclear.

Purpose of the Study:

  • To elucidate the structural and functional interactions between Ca(V)1.2 C-terminal tail and Ca(2+)/CaM.
  • To determine the stoichiometry and assembly state of the Ca(V)1.2-CaM complex.
  • To investigate the differential binding properties of CaM to distinct regions of the Ca(V)1.2 tail.

Main Methods:

  • X-ray crystallography to determine complex structure.
  • Sedimentation equilibrium and subunit-counting experiments for stoichiometry and assembly state.
  • Isothermal titration calorimetry and biochemical assays for binding properties.
  • Electrophysiology to assess functional roles.

Main Results:

  • A Ca(2+)/CaM complex with Ca(V)1.2 C-terminal tail was structurally characterized, revealing two Ca(2+)/CaMs binding to two PreIQ helices and IQ domains.
  • Stoichiometry confirmed as 2:1 Ca(2+)/CaM to C-terminal tail; Ca(V)1.2s exist as monomers in cell membranes, refuting crystallographic dimer relevance.
  • Differential CaM binding observed: Ca(2+)/CaM at the PreIQ C-region is labile, while Ca(2+)/CaM at the IQ domain is stable; apo-CaM shows weak PreIQ interaction.
  • Electrophysiological data indicate the PreIQ C-region's role in calcium-dependent facilitation.

Conclusions:

  • Two Ca(2+)/CaMs can bind simultaneously to the Ca(V)1.2 tail.
  • A functional role for Ca(2+)/CaM binding at the C-region site is established.
  • The study clarifies the Ca(V)1.2-CaM interaction stoichiometry and functional significance, challenging previous models.