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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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G Protein-coupled Receptors01:15

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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

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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.
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Activation and Inactivation of G Proteins01:22

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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 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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GPCR Desensitization01:12

GPCR Desensitization

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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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Related Experiment Video

Updated: Dec 20, 2025

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
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Structural features of activated GPCR signaling complexes.

Jingjing Wang1, Tian Hua2, Zhi-Jie Liu1

  • 1iHuman Institute, ShanghaiTech University, Shanghai 201210, China; School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.

Current Opinion in Structural Biology
|June 3, 2020
PubMed
Summary

This review details G protein-coupled receptor (GPCR) signaling complexes, focusing on structural insights from cryo-electron microscopy (Cryo-EM). It highlights rhodopsin-like GPCR activation and interactions with G proteins and arrestins.

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Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
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Last Updated: Dec 20, 2025

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Strategic Screening and Characterization of the Visual GPCR-mini-G Protein Signaling Complex for Successful Crystallization
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Strategic Screening and Characterization of the Visual GPCR-mini-G Protein Signaling Complex for Successful Crystallization

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Area of Science:

  • Structural biology
  • Molecular pharmacology
  • Biochemistry

Background:

  • G protein-coupled receptors (GPCRs) are crucial cell surface receptors involved in diverse physiological processes.
  • GPCRs activate intracellular signaling cascades through heterotrimeric G proteins or regulatory proteins like arrestins.
  • Recent advancements in cryo-electron microscopy (Cryo-EM) have enabled high-resolution structural determination of GPCR signaling complexes.

Purpose of the Study:

  • To review and summarize reported structures of GPCR-G protein and GPCR-arrestin complexes.
  • To emphasize the structural features governing rhodopsin-like GPCR activation.
  • To elucidate the molecular mechanisms of G protein and arrestin binding to activated GPCRs.

Main Methods:

  • Compilation and analysis of published cryo-electron microscopy (Cryo-EM) structural data.
  • Focus on structural comparisons of rhodopsin-like GPCRs in complex with G proteins and arrestins.
  • Integration of structural findings to interpret signaling mechanisms.

Main Results:

  • Numerous GPCR-G protein and GPCR-arrestin complex structures have been determined using Cryo-EM.
  • Key structural differences and similarities in activation mechanisms of rhodopsin-like GPCRs are identified.
  • Detailed insights into the distinct binding interfaces and conformational changes upon G protein and arrestin engagement are presented.

Conclusions:

  • Cryo-EM has revolutionized our understanding of GPCR signaling complex structures.
  • Structural data provides a molecular basis for understanding GPCR activation and biased signaling.
  • This review consolidates structural knowledge to advance the study of GPCR function and drug discovery.