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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,...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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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Updated: Jun 30, 2026

Applications of Spatio-temporal Mapping and Particle Analysis Techniques to Quantify Intracellular Ca2+ Signaling In Situ
09:34

Applications of Spatio-temporal Mapping and Particle Analysis Techniques to Quantify Intracellular Ca2+ Signaling In Situ

Published on: January 7, 2019

Spatial diffusivity and availability of intracellular calmodulin.

Hugo Sanabria1, Michelle A Digman, Enrico Gratton

  • 1Department of Neurobiology and Anatomy, University of Texas Health Science Center at Houston, Texas 77030, USA.

Biophysical Journal
|September 30, 2008
PubMed
Summary
This summary is machine-generated.

Calmodulin (CaM) diffusion is slowed by binding to target proteins, indicating CaM availability limits signaling. This study quantifies CaM

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Related Experiment Videos

Last Updated: Jun 30, 2026

Applications of Spatio-temporal Mapping and Particle Analysis Techniques to Quantify Intracellular Ca2+ Signaling In Situ
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Published on: January 7, 2019

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Published on: January 23, 2012

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

Area of Science:

  • Cellular signaling and molecular dynamics.
  • Biophysics and biochemistry of protein interactions.

Background:

  • Calmodulin (CaM) is a key transducer of intracellular calcium (Ca2+) signals.
  • CaM forms networks with target proteins to regulate downstream enzyme activation.
  • Spatial and temporal tuning of CaM signaling is crucial for cellular function.

Purpose of the Study:

  • To quantify the spatial diffusivity and availability of CaM under basal and elevated Ca2+ conditions.
  • To investigate the impact of target proteins on CaM diffusion and binding stoichiometry.
  • To assess the role of Ca2+ levels in modulating CaM complex dynamics.

Main Methods:

  • Utilized enhanced green fluorescent protein-labeled CaM (eGFP-CaM) for visualization.
  • Employed raster image scanning spectroscopy and number and brightness analysis.
  • Quantified diffusion rates and binding stoichiometry in living cells.

Main Results:

  • Cytoplasmic eGFP-CaM diffuses twofold slower than eGFP, indicating binding to partners.
  • Coexpression of Ca2+/CaM-dependent protein kinase II significantly reduces eGFP-CaM diffusion.
  • Ca2+/CaM-dependent protein kinase II increases CaM binding stoichiometry to an average of 3 CaMs per diffusive molecule.
  • Elevated intracellular Ca2+ had minimal impact on CaM complex diffusion.

Conclusions:

  • CaM diffusion is spatially modulated by its target proteins.
  • CaM availability is a limiting factor in CaM-signaling networks.
  • These findings contribute to understanding the spatial regulation of Ca2+ signaling pathways.