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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,...
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory organs,...
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
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...
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...

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Related Experiment Video

Updated: May 11, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Calmodulin in a heartbeat.

Anders B Sorensen1, Mads T Søndergaard, Michael T Overgaard

  • 1Department of Biotechnology, Chemistry and Environmental Engineering, Aalborg University, Denmark.

The FEBS Journal
|May 14, 2013
PubMed
Summary

Calmodulin mutations cause heart arrhythmias and sudden death by affecting its interactions with cardiac proteins. Understanding these specific interactions is key to explaining the cardiac-specific effects of these mutations.

Keywords:
arrhythmiacalcium signallingcalmodulincardiomyocytedisease mutation

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Measurement of Calcium Fluctuations Within the Sarcoplasmic Reticulum of Cultured Smooth Muscle Cells Using FRET-based Confocal Imaging

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Last Updated: May 11, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Measurement of Calcium Fluctuations Within the Sarcoplasmic Reticulum of Cultured Smooth Muscle Cells Using FRET-based Confocal Imaging
10:05

Measurement of Calcium Fluctuations Within the Sarcoplasmic Reticulum of Cultured Smooth Muscle Cells Using FRET-based Confocal Imaging

Published on: June 20, 2016

Area of Science:

  • Molecular biology
  • Cardiology
  • Biochemistry

Background:

  • Calmodulin is a crucial calcium sensor in eukaryotic cells, essential for interpreting calcium signaling.
  • It is a highly conserved protein, encoded by three human genes, with significant conformational plasticity.
  • Recent studies link calmodulin mutations to severe cardiac conditions like arrhythmia and sudden cardiac death.

Purpose of the Study:

  • To explore how calmodulin mutations lead to cardiac-specific phenotypes.
  • To identify specific cardiac target proteins affected by these mutations.
  • To understand the molecular mechanisms underlying calmodulin mutation-induced cardiac events.

Main Methods:

  • Review of existing literature on calmodulin function and mutations.
  • Analysis of calmodulin's role in the cardiac contraction cycle.
  • Focus on protein-protein interactions modulated by calmodulin.

Main Results:

  • Calmodulin interacts with numerous proteins, influencing diverse cellular processes.
  • Specific cardiac proteins involved in the contraction cycle are modulated by calmodulin.
  • The conformational plasticity of calmodulin allows for specialized interactions.

Conclusions:

  • Calmodulin mutations can disrupt cardiac function, leading to arrhythmia and sudden death.
  • Specific interactions between mutated calmodulin and cardiac proteins are likely responsible for the observed phenotypes.
  • Further research into these cardiac-specific interactions is needed to elucidate the pathogenic mechanisms.