Calcium Calmodulin Complex

The calcium-calmodulin complex is a calcium-dependent signaling molecule that translates changes in intracellular calcium concentration into cellular responses. When calcium ions bind to calmodulin’s EF-hand domains, the protein undergoes a conformational change that exposes interaction surfaces for target enzymes, ion channels, and regulatory proteins. By activating or modulating these targets, the complex influences processes such as muscle contraction, secretion, metabolism, gene expression, and cell movement. Studying calcium-calmodulin signaling helps explain how cells coordinate rapid responses and provides a foundation for investigating neurological function, immune regulation, cardiovascular biology, and diseases linked to disrupted calcium signaling.

Calcium Calmodulin Complex - Related Videos

Research

JoVE Journal - Biology

Pull-down of Calmodulin-binding Proteins

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Cited by 19 •

2012

Calmodulin (CaM) pull-down assay is an effective way to investigate the interaction of CaM with various proteins. This method uses CaM-sepharose beads for efficient and specific analysis of CaM-binding proteins. This provides an important tool to explore CaM signaling in cellular function.

Education

JoVE Core - Cell Biology

Calmodulin-dependent Signaling

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2023

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,...

Drosophila In Vivo Calcium Imaging: A Method for Functional Imaging of Neuronal Activity

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2023

This video describes in vivo calcium imaging in Drosophila neurons using GCaMP. The featured protocol clip shows how to record changes in GCaMP fluorescence from mushroom body neurons during an olfactory conditioning experiment.

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method

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Cited by 4 •

2016

The Tandem Affinity Purification (TAP) method has been used extensively to isolate native complexes from cellular extract, primarily eukaryotic, for proteomics. Here, we present a TAP method protocol optimized for purification of native complexes for structural studies.

Research

JoVE Journal - Biology
Free Sample

Monitoring Dynamic Changes In Mitochondrial Calcium Levels During Apoptosis Using A Genetically Encoded Calcium Sensor

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Cited by 10 •

2011

This protocol describes a method for real-time measurement of mitochondrial calcium fluxes by fluorescent imaging. The method takes advantage of a circularly permutated YFP-based dual-excitation ratiometric calcium sensor (ratiometric pericam-mt) selectively expressed in mitochondria.

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