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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,...
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...

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Related Experiment Video

Updated: Jun 26, 2026

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+
12:30

Monitoring ER/SR Calcium Release with the Targeted Ca2+ Sensor CatchER+

Published on: May 19, 2017

Generation of a calmodulin-based EPR calcium indicator.

Junlong Shao1, John Cieslak, Adrian Gross

  • 1Department of Molecular Pharmacology and Biological Chemistry, Northwestern University Medical School, 303 East Chicago Avenue, Chicago, Illinois 60611, USA.

Biochemistry
|January 1, 2009
PubMed
Summary
This summary is machine-generated.

Researchers developed spin-labeled calmodulin as a novel calcium indicator. This tool visualizes calcium-dependent protein conformational changes and signals, advancing molecular dynamics studies.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Calmodulin is a key calcium-binding protein mediating cellular responses.
  • Calcium signals are crucial for numerous cellular processes.
  • Understanding calmodulin's conformational dynamics is vital for cell signaling research.

Purpose of the Study:

  • To develop a novel method for detecting calcium-dependent conformational changes in calmodulin.
  • To utilize Electron Paramagnetic Resonance (EPR) spectroscopy for probing protein dynamics.
  • To establish spin-labeled calmodulin as a sensitive calcium indicator.

Main Methods:

  • Site-directed spin labeling to introduce nitroxide EPR probes into calmodulin.
  • Utilizing EPR spectroscopy to monitor calcium-induced conformational changes.
  • Combining spin-labeled calmodulin with flash photolysis of a caged calcium compound.

Main Results:

  • Successfully introduced EPR probes into calmodulin, enabling detection of conformational changes.
  • Demonstrated that spin-labeled calmodulin acts as a sensitive calcium indicator.
  • Showcased the ability to visualize rapid calcium release using flash photolysis and spin-labeled calmodulin.

Conclusions:

  • Spin-labeled calmodulin provides a powerful tool for studying calcium-dependent protein dynamics.
  • EPR spectroscopy offers a valuable approach for molecular-level investigations of calcium signaling.
  • This work represents a significant advancement in understanding protein conformational changes.