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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,...
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
Microtubule Associated Proteins (MAPs)01:42

Microtubule Associated Proteins (MAPs)

Microtubule function and architecture are regulated by an array of specialized proteins called microtubule-associated proteins or MAPs. These proteins are widespread across different organisms and have conserved protein motifs, like the multi-TOG domain for tubulin binding found in the CLASP family of MAPs. Some MAPs are lineage-specific based on their conserved domains. Their functions depend upon the cytoskeletal architecture and cell type they are located within. In-plant cells, a specific...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

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Related Experiment Video

Updated: Jun 12, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Calmodulin-binding proteins in brain.

S Kakiuchi1

  • 1Department of Neurochemistry and Neuropharmacology, Institute of Higher Nervous Activity, Osaka University Medical School, Kita-ku, Osaka 530, Japan.

Neurochemistry International
|May 22, 2010
PubMed
Summary
This summary is machine-generated.

Brain contains abundant calmodulin, a calcium-binding protein. Many calmodulin-binding proteins, crucial for cellular functions, have been identified, suggesting novel regulatory roles in the brain.

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Last Updated: Jun 12, 2026

Pull-down of Calmodulin-binding Proteins
07:51

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Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
08:06

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Modified Roller Tube Method for Precisely Localized and Repetitive Intermittent Imaging During Long-term Culture of Brain Slices in an Enclosed System
09:52

Modified Roller Tube Method for Precisely Localized and Repetitive Intermittent Imaging During Long-term Culture of Brain Slices in an Enclosed System

Published on: December 28, 2017

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Intracellular calcium (Ca2+) signaling is primarily mediated by calmodulin, a ubiquitous Ca2+-binding protein.
  • The brain exhibits a high concentration of calmodulin, significantly exceeding that required for known calmodulin-activated enzymes.
  • A substantial portion of brain calmodulin is associated with various calmodulin-binding proteins (CBPs) that lack intrinsic enzymatic activity.

Purpose of the Study:

  • To investigate the roles of newly discovered calmodulin-binding proteins in the brain.
  • To explore the functional implications of Ca2+-dependent interactions between calmodulin and these associated proteins.
  • To understand the potential regulatory mechanisms involving CBPs in neuronal function.

Main Methods:

  • Identification and characterization of calmodulin-binding proteins in brain tissue.
  • Analysis of Ca2+-dependent associations between calmodulin and identified proteins.
  • Investigating the biochemical properties and cellular localization of key CBPs.

Main Results:

  • Several novel calmodulin-binding proteins were identified in the brain, including calcineurin, tubulin, tau factor, and calspectin.
  • These CBPs exhibit Ca2+-dependent binding to calmodulin, suggesting a regulatory role.
  • Calcineurin demonstrated protein phosphatase activity, while tau factor and calspectin showed interactions with cytoskeleton components like tubulin and F-actin.

Conclusions:

  • Calmodulin-binding proteins play significant, yet largely unelucidated, roles in brain function.
  • These proteins offer potential mechanisms for Ca2+-calmodulin regulation of cellular processes, including cytoskeleton dynamics and axonal transport.
  • Further research into the properties and functions of brain CBPs is essential for understanding Ca2+/calmodulin-mediated regulation in the nervous system.