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Related Concept Videos

Channel Rhodopsins01:11

Channel Rhodopsins

Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
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...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
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...
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...

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Related Experiment Video

Updated: May 23, 2026

FM Dye Cycling at the Synapse: Comparing High Potassium Depolarization, Electrical and Channelrhodopsin Stimulation
08:31

FM Dye Cycling at the Synapse: Comparing High Potassium Depolarization, Electrical and Channelrhodopsin Stimulation

Published on: May 24, 2018

Ryanodine receptor calcium release channels: an evolutionary perspective.

John J Mackrill1

  • 1Department of Physiology, University College Cork, Western Gateway Building, Western Road, Cork, Ireland. j.mackrill@ucc.ie

Advances in Experimental Medicine and Biology
|March 29, 2012
PubMed
Summary

Ryanodine receptors (RyRs) and inositol 1,4,5-trisphosphate receptors (IP(3)Rs) are calcium-releasing channels. This study surveys RyR-like genes across diverse taxa, proposing an evolutionary model involving horizontal gene transfer.

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Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
11:31

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

Related Experiment Videos

Last Updated: May 23, 2026

FM Dye Cycling at the Synapse: Comparing High Potassium Depolarization, Electrical and Channelrhodopsin Stimulation
08:31

FM Dye Cycling at the Synapse: Comparing High Potassium Depolarization, Electrical and Channelrhodopsin Stimulation

Published on: May 24, 2018

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
11:31

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Ryanodine receptors (RyRs) and inositol 1,4,5-trisphosphate receptors (IP(3)Rs) are crucial for intracellular calcium (Ca2+) release in eukaryotes.
  • Ca2+ acts as a fundamental second messenger, regulating numerous cellular processes.
  • Vertebrates have multiple RYR genes, while other multicellular organisms have one, and RyR-like channels are found in unicellular organisms.

Purpose of the Study:

  • To provide an overview of RyR-like gene expression across a wide range of viral, archaeal, bacterial, and eukaryotic taxa.
  • To analyze the structural and phylogenetic relationships of these proteins.
  • To propose a model for the early evolution of RyR proteins.

Main Methods:

  • Exploitation of expanded genome data.
  • Analysis of multidomain structures of RyR-like proteins.
  • Phylogenetic analysis of RyR-like proteins.

Main Results:

  • RyR-like genes are expressed across a broad spectrum of life, from viruses to eukaryotes.
  • Structural and phylogenetic analyses reveal conserved domains and evolutionary relationships.
  • A model is proposed for the evolution of RyR from IP(3)R-like channels.

Conclusions:

  • The evolution of RyR proteins likely involved the acquisition of promiscuous protein domains, potentially through horizontal gene transfer.
  • This evolutionary event occurred early in eukaryotic evolution.
  • RyR-like channels exhibit a wide distribution across different biological domains.