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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...
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...
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Updated: May 31, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Calmodulin overexpression does not alter Cav1.2 function or oligomerization state.

Felix Findeisen1, Alexandra Tolia, Ryan Arant

  • 1Cardiovascular Research Institute, University of California, San Francisco, USA.

Channels (Austin, Tex.)
|June 30, 2011
PubMed
Summary
This summary is machine-generated.

Calmodulin (CaM) interactions with voltage-gated calcium channels (Ca(v)1.2) do not form multimers. Further evidence supports a monomeric Ca(v)1.2 channel stoichiometry, with CaM binding potentially influencing channel function.

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Area of Science:

  • Molecular and Cellular Biology
  • Neuroscience
  • Biophysics

Background:

  • Calmodulin (CaM) and voltage-gated calcium channels (Ca(v)s) are critical for cellular calcium signaling.
  • Previous structural data suggested a Ca(v)1.2 C-terminal tail complex with a 4:2 Ca(2+)/CaM:Ca(v) stoichiometry.

Purpose of the Study:

  • To investigate the stoichiometry of Ca(v)1.2 channels and their interaction with Ca(2+)/CaM.
  • To determine if Ca(v)1.2 channels form multimers as suggested by crystallographic data.

Main Methods:

  • Biochemical analysis
  • Subunit counting experiments in live cell membranes
  • CaM overexpression studies
  • Analysis of electrostatic surfaces

Main Results:

  • CaM overexpression did not affect Ca(v)1.2 inactivation or channel stoichiometry.
  • Biochemical and live cell experiments did not support the formation of 4:2 Ca(2+)/CaM:Ca(v) complexes.
  • Data strongly support a monomeric stoichiometry for full-length Ca(v)1.2 channels.

Conclusions:

  • The findings refute the proposed multimeric Ca(v)1.2-CaM complex.
  • Evidence supports a monomeric Ca(v)1.2 channel structure.
  • Electronegative patches on the Ca(v)1.2 C-terminal tail may mediate interactions with other intracellular domains, influencing channel modulation.