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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,...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
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...
Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
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Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
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Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...

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Updated: Jul 13, 2026

Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients
08:15

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

Published on: July 16, 2018

Calcium-induced phospholipid ordering depends on surface pressure.

Maria Sovago1, George W H Wurpel, Marc Smits

  • 1FOM Institute for Atomic and Molecular Physics (AMOLF), Kruislaan 407, 1098 SJ, Amsterdam, The Netherlands.

Journal of the American Chemical Society
|August 19, 2007
PubMed
Summary

Calcium ions significantly alter phospholipid monolayers, inducing ordered domains at low pressures and disorder at intermediate pressures. At high pressures, calcium expands and orders lipid chains, affecting both zwitterionic and anionic lipids.

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Atomic Force Microscopy Imaging and Force Spectroscopy of Supported Lipid Bilayers
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Atomic Force Microscopy Imaging and Force Spectroscopy of Supported Lipid Bilayers

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Last Updated: Jul 13, 2026

Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients
08:15

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

Published on: July 16, 2018

Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator
07:11

Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator

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Atomic Force Microscopy Imaging and Force Spectroscopy of Supported Lipid Bilayers
10:15

Atomic Force Microscopy Imaging and Force Spectroscopy of Supported Lipid Bilayers

Published on: July 22, 2015

Area of Science:

  • Biophysics
  • Surface Chemistry
  • Materials Science

Background:

  • Phospholipid monolayers are crucial in biological membranes and nanotechnology.
  • Understanding ion interactions with lipid interfaces is key to controlling their properties.

Purpose of the Study:

  • To investigate the impact of sodium and calcium ions on zwitterionic and anionic phospholipid monolayers.
  • To elucidate the pressure-dependent effects of calcium ions on monolayer structure and organization.

Main Methods:

  • Vibrational sum-frequency generation spectroscopy.
  • Surface pressure measurements.
  • Fluorescence microscopy.

Main Results:

  • Calcium ions (Ca2+) exert a significant, pressure-dependent influence on phospholipid monolayers.
  • Ca2+ induced ordered domains at low surface pressures (~5 mN/m) and disorder at intermediate pressures (5-25 mN/m).
  • At high pressures (>25 mN/m), Ca2+ expanded monolayers while ordering lipid chains, with similar effects observed for both zwitterionic and anionic lipids.

Conclusions:

  • Calcium ion complexation with phospholipids is strongly dependent on surface pressure.
  • The observed effects suggest specific molecular interactions between Ca2+ and lipid headgroups.
  • These findings offer insights into ion-lipid interactions relevant to biological systems and material design.