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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,...
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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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Pull-down of Calmodulin-binding Proteins
07:51

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Published on: January 23, 2012

The Ca(2+) influence on calmodulin unfolding pathway: a steered molecular dynamics simulation study.

Yong Zhang1, Jizhong Lou

  • 1Laboratory of Non-Coding RNAs, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.

Plos One
|November 13, 2012
PubMed
Summary

Calcium (Ca2+) significantly alters calmodulin (CaM) unfolding dynamics. The N-terminal domain unfolds first in Ca2+-loaded CaM, while the C-terminal domain unfolds first in Ca2+-free CaM, revealing key unfolding barriers.

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Computational Chemistry

Background:

  • Calmodulin (CaM) is a crucial calcium-binding protein involved in numerous cellular processes.
  • Understanding CaM's mechanical properties, particularly its force-induced unfolding, is vital for elucidating its function.
  • Previous studies have explored CaM's behavior, but atomistic details of its force-induced unfolding remain incompletely understood.

Purpose of the Study:

  • To investigate the atomistic details of force-induced calmodulin unfolding using steered molecular dynamics.
  • To determine the influence of calcium (Ca2+) on CaM's stability and unfolding pathways.
  • To compare simulation results with experimental observations from atomic force microscopy (AFM).

Main Methods:

  • Steered molecular dynamics simulations were employed to model the force-induced unfolding of CaM.
  • Simulations included isolated CaM domains and full-length CaM under various N-C-terminal pulling schemes.
  • Both Ca(2+)-loaded and Ca(2+)-free CaM were simulated to assess the role of calcium ions.

Main Results:

  • Calcium ions significantly impact the stability and unfolding behavior of CaM domains and full-length CaM.
  • In Ca(2+)-loaded CaM, the N-terminal domain unfolds before the C-terminal domain.
  • In Ca(2+)-free CaM, the unfolding order is reversed, with the C-terminal domain unfolding first.
  • The primary unfolding barrier in both domains arises from the interaction of EF-hand motifs.

Conclusions:

  • The study provides atomistic-level insights into the force-induced unfolding of calmodulin.
  • The findings explain experimental observations related to CaM's mechanical response.
  • The differential unfolding order based on Ca(2+) presence highlights the ion's critical regulatory role.