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Calmodulin-dependent Signaling

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 Concentration

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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.
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Related Experiment Video

Updated: Mar 25, 2026

Ex Vivo Imaging of Cell-specific Calcium Signaling at the Tripartite Synapse of the Mouse Diaphragm

Ex Vivo Imaging of Cell-specific Calcium Signaling at the Tripartite Synapse of the Mouse Diaphragm

Published on: October 4, 2018

EF-Hand Mimicking Calcium Binding Polymer.

Hee Jung Chung¹, Du Young Ko¹, Hyo Jung Moon¹

¹Department of Chemistry and Nanoscience, Ewha Womans University , 52 Ewhayeodae-gil, Seodaemun-gu, Seoul 120-750, Korea.

Biomacromolecules

|February 25, 2016

Summary

This summary is machine-generated.

Researchers synthesized a calcium binding polymer (CBP) mimicking calmodulin's EF-hand structure. This CBP demonstrates similar Ca(2+) binding affinity and selectivity, showing potential for biomimetic calcium-binding applications.

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Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients

Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients

Published on: July 16, 2018

Area of Science:

Biomaterials Science
Polymer Chemistry
Biochemistry

Background:

Calmodulin is a ubiquitous calcium-binding protein crucial for Ca(2+)-mediated signal transduction.
EF-hand polypeptides within calmodulin possess carboxylate groups that bind calcium ions.
Mimicking natural calcium-binding motifs is a key strategy in developing synthetic calcium-binding materials.

Purpose of the Study:

To synthesize a novel calcium binding polymer (CBP) that mimics the EF-hand structure of calmodulin.
To characterize the Ca(2+) binding properties, including affinity and selectivity, of the synthesized CBP.
To compare the CBP's Ca(2+) binding characteristics with those of natural calmodulin.

Main Methods:

Synthesis of a poly(L-alanine)-poly(L-alanine-co-L-glutamic acid)-poly(ethylene glycol)-poly(L-alanine-co-L-glutamic acid)-poly(L-alanine) (PA-PAE-PEG-PAE-PA) polymer.
Circular dichroism (CD) and 13C Nuclear Magnetic Resonance (NMR) spectroscopy to detect conformational changes upon Ca(2+) binding.
Competitive binding assays using 5,5-Br2-BAPTA and murexide to determine binding constants and selectivity for Ca(2+), Cu(2+), and Zn(2+).

Main Results:

The synthesized CBP exhibited conformational changes upon Ca(2+) binding, as evidenced by CD and NMR spectra.
The binding constant of CBP for Ca(2+) was determined to be 5.1 × 10(5) M(-1), comparable to calmodulin.
CBP showed 2-4 fold higher selectivity for Ca(2+) over Cu(2+) and Zn(2+), with binding constants of 7.0 × 10(5) M(-1) for Ca(2+), 4.2 × 10(5) M(-1) for Cu(2+), and 1.7 × 10(5) M(-1) for Zn(2+).

Conclusions:

The synthesized CBP effectively mimics the calcium-binding properties of calmodulin's EF-hand motif.
The polymer demonstrates significant affinity and selectivity for Ca(2+), suggesting its potential as a biomimetic calcium-binding material.
This study provides a foundation for designing synthetic polymers with tailored calcium-binding capabilities for various applications.