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Related Concept Videos

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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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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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
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Understanding the Structural Basis of Adhesion GPCR Functions.

Demet Araç1, Norbert Sträter2, Elena Seiradake3

  • 1Department of Biochemistry and Molecular Biology, University of Chicago, 929 E. 57th Street, GCIS W210, Chicago, IL, 60637, USA. arac@uchicago.edu.

Handbook of Experimental Pharmacology
|November 11, 2016
PubMed
Summary

Adhesion GPCRs (aGPCRs) possess unique, large extracellular regions that are cleaved and influence receptor function. This review explores their structure and potential roles in ligand binding and activation.

Keywords:
FLRTGAINHormLatrophilinLectinOlfactomedinStachelSuper-complexTethered agonistUnc5

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Adhesion GPCRs (aGPCRs) differ from conventional GPCRs due to large extracellular regions.
  • These regions undergo autoproteolytic cleavage within the conserved GPCR-Autoproteolysis INducing (GAIN) domain.
  • The extracellular regions contain variable domains crucial for ligand adhesion.

Purpose of the Study:

  • To summarize the current structural understanding of aGPCR extracellular regions.
  • To discuss the functional roles of these extracellular regions based on structural insights.

Main Methods:

  • Literature review of structural and functional studies on aGPCR extracellular regions.

Main Results:

  • aGPCRs feature large, cleaved extracellular regions with conserved GAIN domains and variable ligand-binding modules.
  • Structural information reveals how these regions are juxtaposed to the transmembrane domain.
  • Emerging evidence indicates extracellular regions modulate aGPCR function and activation.

Conclusions:

  • The structural diversity of aGPCR extracellular regions suggests specialized ligand interactions.
  • Understanding aGPCR structure is key to elucidating their diverse physiological roles.
  • Further research into extracellular region structure-function relationships will advance aGPCR knowledge.