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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,...
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...
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...

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Related Experiment Video

Updated: May 22, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Structural basis for calmodulin as a dynamic calcium sensor.

Miao Zhang1, Cameron Abrams, Liping Wang

  • 1Department of Molecular Physiology and Biophysics, Jefferson Medical College, Philadelphia, PA 19107, USA.

Structure (London, England : 1993)
|May 15, 2012
PubMed
Summary
This summary is machine-generated.

Target proteins dynamically alter calmodulin's Ca(2+) binding affinity. This research reveals how calmodulin acts as a flexible sensor, adapting to varying calcium levels in cellular signaling pathways.

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Area of Science:

  • Molecular biology
  • Cellular signaling
  • Biochemistry

Background:

  • Calmodulin (CaM) is a crucial calcium (Ca2+) sensor in all eukaryotic cells, mediating Ca2+-dependent signaling pathways.
  • CaM undergoes conformational changes upon Ca2+ binding, enabling interaction with diverse target proteins.
  • The precise mechanisms by which target proteins modulate CaM's Ca2+ binding properties remain largely unexplored.

Purpose of the Study:

  • To investigate how target proteins influence calmodulin's Ca2+ binding affinity and conformation.
  • To elucidate the role of SK2 channel splice variants in regulating CaM's Ca2+ sensing capabilities.

Main Methods:

  • Utilized two splice variants of SK2 channels with differing Ca2+ sensitivities.
  • Employed protein crystal structures and experimental analyses.
  • Characterized CaM conformations and Ca2+ binding affinities in complex with SK2 variants.

Main Results:

  • Calmodulin exhibits distinct C-lobe conformations and Ca2+ binding affinities when interacting with different SK2 splice variants.
  • Target protein binding induces significant conformational plasticity in calmodulin.
  • These target-induced changes enable calmodulin to function as a dynamic Ca2+ sensor.

Conclusions:

  • Target proteins play a critical role in regulating calmodulin's Ca2+ sensitivity.
  • Calmodulin's dynamic conformational changes allow for precise tuning of cellular Ca2+ signaling responses.
  • This study provides new insights into the adaptability of Ca2+ sensing mechanisms.