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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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,...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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 affinity and are together...
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...
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

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.
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

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.
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

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, 7TM, or...

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Imaging G-protein Coupled Receptor (GPCR)-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum
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Dimerization in GPCR mobility and signaling.

Martin J Lohse1

  • 1Institute of Pharmacology and Toxicology, Würzburg, Germany. lohse@toxi.uni-wuerzburg.de

Current Opinion in Pharmacology
|November 14, 2009
PubMed
Summary
This summary is machine-generated.

G-protein-coupled receptors (GPCRs) can form dimers, influencing their cell surface mobility and intracellular trafficking. While not essential for ligand binding or signaling, dimerization may modulate GPCR functions.

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Imaging G-protein Coupled Receptor (GPCR)-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum
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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

Published on: March 16, 2020

Area of Science:

  • Molecular biology
  • Cell biology
  • Biochemistry

Background:

  • Many DNA-binding receptors function as dimers, enhancing ligand specificity and signaling.
  • G-protein-coupled receptors (GPCRs) were traditionally considered monomeric, but recent evidence suggests dimerization.
  • The physiological relevance and conditions for GPCR dimerization remain under investigation.

Purpose of the Study:

  • To explore the role and implications of G-protein-coupled receptor (GPCR) dimerization.
  • To understand how GPCR dimerization affects receptor behavior and signaling.

Main Methods:

  • Literature review of recent evidence on GPCR dimerization.
  • Analysis of studies investigating GPCR complex formation.

Main Results:

  • GPCR dimerization is increasingly recognized, though its occurrence under physiological conditions is uncertain.
  • GPCR dimerization is generally not required for ligand recognition or signal initiation.
  • Dimerization appears to influence GPCR cell surface mobility, intracellular trafficking, and signaling modulation.

Conclusions:

  • GPCR dimerization plays a role beyond basic ligand binding and activation.
  • Dimerization may fine-tune GPCR function, affecting receptor localization and downstream effects.
  • Further research is needed to fully elucidate the physiological significance of GPCR dimerization.