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Related Concept Videos

Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
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,...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Cell-surface Signaling01:21

Cell-surface Signaling

Hormones—or any molecule that binds to a receptor, known as a ligand—that are lipid-insoluble (water-soluble) are not able to diffuse across the cell membrane. In order to be able to affect a cell without entering it, these hormones bind to receptors on the cell membrane. When a first messenger, a hormone, binds to a receptor, a signal cascade is set off, causing second messengers, proteins inside the cell, to become activated, resulting in downstream effects.

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Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators
11:33

Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators

Published on: March 22, 2019

Cell surface topology creates high Ca2+ signalling microdomains.

Jens Christian Brasen1, Lars Folke Olsen, Maurice B Hallett

  • 1CelCom, Institute of Biochemistry and Molecular Biology, University of Southern Denmark, Denmark. christianb@bmb.sdu.dk

Cell Calcium
|February 16, 2010
PubMed
Summary

Cellular surface topology, specifically wrinkled membranes, creates high calcium (Ca2+) microdomains. These microdomains, up to 80 microM, resolve the paradox of enzyme activation and impact cell functions.

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Dissection of Local Ca2+ Signals in Cultured Cells by Membrane-targeted Ca2+ Indicators
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Published on: March 22, 2019

Imaging Initial Ca2+ Microdomains in Primary T Cells
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Imaging Local Ca2+ Signals in Cultured Mammalian Cells
09:30

Imaging Local Ca2+ Signals in Cultured Mammalian Cells

Published on: March 3, 2015

Area of Science:

  • Cell Biology
  • Biophysics
  • Biochemistry

Background:

  • Cellular microdomains are crucial for processes like calcium (Ca2+) signaling.
  • Cytosolic Ca2+ levels measured are typically low (< few micromolar), yet some enzymes require >20 microM Ca2+ for activation.

Purpose of the Study:

  • To resolve the paradox between low cytosolic Ca2+ and high enzyme activation requirements.
  • To investigate the role of cell surface topology in generating high Ca2+ microdomains.

Main Methods:

  • Computational modeling of Ca2+ diffusion within cellular environments.
  • Simulations using both smooth and wrinkled cell surface models.
  • Analysis of Ca2+ concentration gradients in different membrane wrinkle geometries.

Main Results:

  • A wrinkled cell surface topology significantly enhances Ca2+ microdomain formation compared to a smooth surface.
  • Simulations predict Ca2+ concentrations up to 80 microM within membrane wrinkles.
  • High Ca2+ microdomains are most effectively generated by long, narrow wrinkles.

Conclusions:

  • Cell surface topology is a key, previously unrecognized factor in generating high Ca2+ microdomains.
  • Intra-wrinkle Ca2+ concentrations can reach levels sufficient for enzyme activation.
  • These microdomains are strategically located for regulating the cytoskeleton and membrane expansion.