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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,...

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Related Experiment Video

Updated: Jun 2, 2026

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

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

Published on: May 19, 2017

Redesign of Calmodulin for Genetically Encoded Zn²⁺ Sensing with High Dynamic Range.

Chunhong Liu¹, Qingyuan Hu¹, Li Jin²

¹State Key Laboratory of Coordination Chemistry, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210023, China.

Chemical & Biomedical Imaging

|June 1, 2026

Summary

Researchers engineered a new genetically encoded zinc sensor (mNG-ZnM1.0) by modifying a calcium indicator. This advanced biosensor offers high dynamic range and selectivity for detecting zinc ions in vitro and in live cells.

Keywords:

Calmodulin Dynamic range EF-hand motifs Fluorescence imaging Genetically encoded biosensor Zinc

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Last Updated: Jun 2, 2026

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Published on: February 7, 2018

Area of Science:

Biochemistry and Molecular Biology
Biosensor Development
Genetically Encoded Probes

Background:

Genetically encoded zinc probes (GEZPs) face limitations due to inefficient signal transduction from natural zinc-binding domains.
Existing calcium indicators leverage calmodulin (CaM) for superior dynamic range through cooperative conformational changes.

Purpose of the Study:

To rationally redesign calmodulin (CaM) for enhanced zinc (Zn²⁺) sensing capabilities.
To develop a novel biosensor, mNG-ZnM1.0, with high dynamic range and selectivity for Zn²⁺ detection.

Main Methods:

Mutagenesis of CaM's EF-hand motifs (e.g., to cysteine or histidine) to create Zn²⁺-specific binding sites.
Saturation mutagenesis and directed evolution to optimize Zn²⁺ sensing performance and dynamic range.
In vitro and live-cell assays to evaluate sensor performance, including dynamic range (F_max/F_min) and selectivity.

Main Results:

Developed the mNG-ZnM1.0 biosensor, demonstrating a dynamic range of up to 20-fold in vitro and 4-fold in live cells for Zn²⁺.
The engineered sensor showed comparable or superior performance to existing GEZPs.
Successfully visualized in vivo Zn²⁺ dynamics during zebrafish development.

Conclusions:

mNG-ZnM1.0 represents a significant advancement in GEZPs, offering enhanced Zn²⁺ detection capabilities.
The study provides a successful paradigm for reprogramming protein scaffolds for new functionalities.
Expanded the toolkit for sensing biological ions, enabling new avenues for research in cellular and developmental processes.