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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 affinity and are together...
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Related Experiment Video

Updated: Jul 5, 2026

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
12:43

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

Grb2 adaptor undergoes conformational change upon dimerization.

Caleb B McDonald1, Kenneth L Seldeen, Brian J Deegan

  • 1Department of Biochemistry and Molecular Biology and the UM/Sylvester Braman Family Breast Cancer Institute, Leonard Miller School of Medicine, University of Miami, Gautier Building, Room 214, 1011 NW 15th Street, Miami, FL 33136, USA.

Archives of Biochemistry and Biophysics
|April 30, 2008
PubMed
Summary

Grb2 (Growth factor receptor-bound protein 2) adaptor protein exists in a monomer-dimer balance. This equilibrium, driven by entropy, influences signal transduction fidelity and amplification in cellular pathways.

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Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
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A High-content Imaging Workflow to Study Grb2 Signaling Complexes by Expression Cloning
10:52

A High-content Imaging Workflow to Study Grb2 Signaling Complexes by Expression Cloning

Published on: October 30, 2012

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Signaling

Background:

  • Grb2 (Growth factor receptor-bound protein 2) is a key adaptor protein linking receptor tyrosine kinases to downstream effectors like Ras and Akt.
  • Its role in mitogenic signaling and potential as a therapeutic target highlight the need to understand Grb2 oligomerization.
  • The precise function of Grb2 dimerization in cellular signaling remains largely uncharacterized.

Purpose of the Study:

  • To investigate the oligomerization state of Grb2 in solution.
  • To elucidate the thermodynamic principles governing Grb2 monomer-dimer equilibrium.
  • To explore the structural basis and functional implications of Grb2 dimerization.

Main Methods:

  • Size-exclusion chromatography
  • Mass spectrometry
  • Analytical ultracentrifugation
  • Isothermal titration calorimetry
  • 3D structural modeling

Main Results:

  • Grb2 exists in a monomer-dimer equilibrium in solution.
  • Dimer dissociation is entropically driven with minimal enthalpic change at physiological temperatures.
  • Thermodynamic analysis suggests conformational rearrangement, potentially via domain swapping, upon Grb2 dimerization.
  • Structural models support domain swapping as the mechanism for conformational changes.

Conclusions:

  • Grb2 dimerization is an entropically driven process involving conformational changes.
  • Grb2 oligomerization may enhance signal transduction fidelity and enable rapid signal amplification.
  • This study provides novel insights into Grb2's function as an adaptor in cellular signaling circuitry.