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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.
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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...
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GPCRs Regulate Adenylyl Cylase Activity

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Live Cell Calcium Imaging Combined with siRNA Mediated Gene Silencing Identifies Ca2+ Leak Channels in the ER Membrane and their Regulatory Mechanisms
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Akt regulates L-type Ca2+ channel activity by modulating Cavalpha1 protein stability.

Daniele Catalucci1, Deng-Hong Zhang, Jaime DeSantiago

  • 1Division of Cardiology, Department of Medicine, University of California-San Diego, La Jolla, CA 92093, USA. daniele.catalucci@itb.cnr.it

The Journal of Cell Biology
|March 25, 2009
PubMed
Summary

Protein kinase Akt stabilizes cardiac L-type Ca(2+) channels (LTCCs) by phosphorylating Ca(v)beta2, preventing Ca(v)alpha1 degradation. This increases LTCC density, impacting cardiac calcium handling and contractility.

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Area of Science:

  • Cardiovascular Physiology
  • Molecular Cell Biology
  • Signal Transduction

Background:

  • The insulin/IGF-1/PI3K/Akt pathway influences cardiac function.
  • Akt's role in cardiac contractility is known, but its molecular targets are unclear.
  • Regulation of L-type Ca(2+) channels (LTCCs) is crucial for cardiac calcium handling.

Purpose of the Study:

  • To elucidate the molecular mechanisms by which Akt regulates cardiac LTCCs.
  • To investigate Akt's effect on LTCC protein density and function.
  • To identify novel pathways modulating cardiac contractility.

Main Methods:

  • Investigated Akt-dependent phosphorylation of LTCC subunits.
  • Utilized molecular biology techniques to assess protein degradation pathways.
  • Examined the impact of PEST sequences on Ca(v)alpha1 stability.
  • Measured LTCC density and function in response to Akt modulation.

Main Results:

  • Akt phosphorylates Ca(v)beta2, a key chaperone for LTCCs.
  • Phosphorylation of Ca(v)beta2 prevents the degradation of the Ca(v)alpha1 subunit.
  • PEST sequences in Ca(v)alpha1 are recognized for degradation, but this is inhibited by Akt-mediated phosphorylation.
  • Increased Ca(v)alpha1 stability leads to higher LTCC protein density.
  • Enhanced LTCC density modulates cardiac Ca(2+) channel function and cellular calcium handling.

Conclusions:

  • Akt plays a novel role in regulating LTCC stability via Ca(v)beta2 phosphorylation.
  • This mechanism increases LTCC density, affecting cardiac calcium influx and contractility.
  • The findings reveal a new pathway for modulating cardiac function through LTCC regulation.