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Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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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.
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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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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.
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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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Mapping Dysfunctional Protein-Protein Interactions in Disease
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Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

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Systematic protein-protein interaction mapping for clinically relevant human GPCRs.

Kate Sokolina1, Saranya Kittanakom1, Jamie Snider1

  • 1Donnelly Centre, University of Toronto, Toronto, ON, Canada.

Molecular Systems Biology
|March 17, 2017
PubMed
Summary
This summary is machine-generated.

This study maps the human G-protein-coupled receptor (GPCR) interactome, identifying 686 interacting proteins. This provides a valuable resource for understanding GPCR signaling pathways and developing new therapeutics.

Keywords:
G‐protein‐coupled receptorshigh‐throughput screeningintegrative computational biologyinteractomeprotein–protein interactionssplit‐ubiquitin membrane yeast two‐hybrid assay

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Area of Science:

  • Integral membrane protein research
  • Proteomics and interactomics
  • Cellular signaling pathways

Background:

  • G-protein-coupled receptors (GPCRs) are crucial integral membrane proteins regulating numerous signaling pathways.
  • Their complex nature presents challenges for traditional proteomics studies.
  • Understanding GPCR interactions is vital for drug discovery.

Purpose of the Study:

  • To generate a global map of the human GPCR interactome.
  • To identify novel components and pathways associated with GPCRs.
  • To provide a resource for studying druggable GPCRs.

Main Methods:

  • Utilized a modified membrane yeast two-hybrid (MYTH) approach.
  • Investigated 48 full-length human ligand-unoccupied GPCRs in their native membrane environment.
  • Identified interacting partners and mapped unique interactions.

Main Results:

  • The study identified an interactome connecting 686 proteins via 987 unique interactions.
  • Included 299 membrane proteins involved in diverse cellular functions.
  • Validated novel interactions for GPR37, serotonin 5-HT4d, and adenosine ADORA2A receptors.

Conclusions:

  • This work presents the first large-scale interactome map for human GPCRs.
  • The GPCR interactome serves as a valuable resource for analyzing GPCR signaling.
  • Facilitates the exploration of this druggable protein family for therapeutic targets.