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Related Concept Videos

G-protein Coupled Receptors01:21

G-protein Coupled Receptors

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G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
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G Protein-coupled Receptors01:15

G Protein-coupled Receptors

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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...
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Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

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G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical,...
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Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
4.8K
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

7.2K
Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
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Related Experiment Video

Updated: Sep 8, 2025

Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
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Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding

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Information Transmission and Processing in G-Protein-Coupled-Receptor Complexes.

Roger D Jones1,2,3, Achille Giacometti2,3, Alan M Jones1,4

  • 1Department of Biology University of North Carolina at Chapel Hill Chapel Hill North Carolina 27514 USA.

Arxiv
|August 20, 2025
PubMed
Summary

This study introduces a thermodynamic model for G-protein-coupled receptors (GPCRs) switching behavior. It reveals three stable states controlled by chemical flux and energy differences, advancing understanding of cellular information processing.

Keywords:
G Protein-Coupled Receptor (GPCR)Second Law of Thermodynamicsentropyinduced fitinformation flownonequilibrium steady statephosphatse

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A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
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G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay
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G Protein-selective GPCR Conformations Measured Using FRET Sensors in a Live Cell Suspension Fluorometer Assay
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Area of Science:

  • Biophysics
  • Cellular Biology
  • Theoretical Chemistry

Background:

  • G-protein-coupled receptors (GPCRs) are crucial for cellular signaling but their switching mechanisms are not fully understood.
  • Existing models often overlook the physical principles governing GPCR conformational changes.

Purpose of the Study:

  • To develop a first-principles theoretical framework for GPCR switching behavior.
  • To elucidate the fundamental control parameters governing GPCR states.
  • To explore the implications for biological switching systems.

Main Methods:

  • Developed a theoretical model based on nonequilibrium thermodynamics.
  • Analyzed GPCR switching using light-controlled impedance assays.
  • Incorporated chemical flux and free-energy differences as key parameters.
  • Modeled ligand-derived inputs and phosphatase activity.

Main Results:

  • Predicted three quasi-stable GPCR configurations, optimizing information transmission.
  • Differentiated between active (with flux) and inactive (without flux) states.
  • Identified chemical flux and energy differences as primary control parameters.
  • Demonstrated ligand conformation modulates GPCR states.

Conclusions:

  • The framework provides a new understanding of GPCRs as nonequilibrium chemical flux-driven switches.
  • The model successfully explains experimental data on GPCR state modulation.
  • This approach is generalizable to other biological switching systems.