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Related Concept Videos

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

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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

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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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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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Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
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Activated G Protein Gαs Samples Multiple Endomembrane Compartments.

Brent R Martin1, Nevin A Lambert2

  • 1From the Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109 and.

The Journal of Biological Chemistry
|August 17, 2016
PubMed
Summary

Activated Gαs proteins rapidly move to intracellular membranes like the endoplasmic reticulum and mitochondria. This translocation is not via specific vesicles but involves constitutive endocytosis for endosomal compartments.

Keywords:
G protein-coupled receptor (GPCR)endosomeendosomesheterotrimeric G proteinintracellular traffickinglipaseprotein acylationprotein palmitoylation

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Signal Transduction

Background:

  • Heterotrimeric G proteins mediate extracellular signal transduction at the plasma membrane.
  • G proteins, including Gαs, can translocate to intracellular compartments after activation.
  • The precise mechanisms and destinations of Gαs translocation remain largely unknown.

Purpose of the Study:

  • To investigate the intracellular translocation mechanism and destinations of activated Gαs.
  • To elucidate the pathways involved in Gαs movement between cellular compartments.
  • To understand the role of acylation-deacylation in Gαs localization and internalization.

Main Methods:

  • Bioluminescence Resonance Energy Transfer (BRET) was employed to track Gαs movement in live cells.
  • Analysis of Gαs association with various intracellular organelles post-activation.
  • Investigation of endocytosis and recycling pathways for Gαs.

Main Results:

  • Activated Gαs rapidly associates with the endoplasmic reticulum, mitochondria, and endosomes.
  • Translocation appears to be indiscriminate sampling of intracellular membranes, not a specific vesicular transport.
  • Endosomal Gαs primarily originates from constitutive endocytosis, not activity-dependent internalization.
  • Gαs recycling to the plasma membrane is completed within 25 minutes after stimulation cessation.
  • Acylation-deacylation is crucial for plasma membrane localization but not activity-dependent internalization.

Conclusions:

  • Activated Gαs undergoes rapid, non-specific association with intracellular membranes.
  • Gαs localization is influenced by both constitutive endocytosis and acylation cycles.
  • Understanding Gαs dynamics provides insights into signal transduction regulation.