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Related Concept Videos

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...
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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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Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
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Non-gated Ion Channels01:24

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Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
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CaMKII-induced shift in modal gating explains L-type Ca(2+) current facilitation: a modeling study.

Yasmin L Hashambhoy1, Raimond L Winslow, Joseph L Greenstein

  • 1Institute for Computational Medicine, Center for Cardiovascular Bioinformatics and Modeling, and the Whitaker Biomedical Engineering Institute, the Johns Hopkins University, Baltimore, Maryland, USA.

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Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) facilitates L-type Ca(2+) channel current (I(CaL)) by shifting gating modes. This CaMKII-mediated phosphorylation mechanism explains I(CaL) augmentation during repeated depolarization.

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Area of Science:

  • Cardiovascular Physiology
  • Molecular and Cellular Electrophysiology
  • Biophysical Modeling

Background:

  • L-type Ca(2+) channel (LCC) facilitation enhances Ca(2+) current (I(CaL)) during rapid depolarization.
  • Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is implicated in LCC facilitation.
  • Potential mechanisms include altered inactivation/recovery and shifts in gating modes (mode 1 to mode 2).

Purpose of the Study:

  • To investigate the role of CaMKII-mediated LCC phosphorylation in facilitating I(CaL).
  • To test the hypothesis that a shift in LCC modal gating distribution underlies facilitation.
  • To develop a computational model to simulate these interactions.

Main Methods:

  • Developed a stochastic model of CaMKII, LCCs, and phosphatases.
  • Integrated this into an existing canine ventricular myocyte model.
  • Simulated LCC behavior under varying Ca(2+) and calmodulin levels.

Main Results:

  • The model successfully reproduced I(CaL) facilitation at physiological protein levels.
  • Simulations demonstrated that CaMKII-dependent shifts to mode 2 gating explain the I(CaL) positive staircase.
  • Model results suggest observed changes in inactivation/recovery kinetics arise from modal shifts, not intrinsic property changes.

Conclusions:

  • CaMKII-mediated phosphorylation drives LCCs to a mode 2 gating state, causing facilitation.
  • Modal gating shifts are the primary mechanism for I(CaL) augmentation.
  • The developed model is a valuable tool for interpreting experimental I(CaL) data.