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Related Concept Videos

GTPases and their Regulation02:14

GTPases and their Regulation

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Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
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Small GTPases - Ras and Rho01:24

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Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
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The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
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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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Related Experiment Video

Updated: Aug 2, 2025

Peptides from Phage Display Library Modulate Gene Expression in Mesenchymal Cells and Potentiate Osteogenesis in Unicortical Bone Defects
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Targeted Proteomic Profiling Revealed Roles of Small GTPases during Osteogenic Differentiation.

Yen-Yu Yang1, Ruthia Soh2, Madeline Vera-Colón3

  • 1Department of Chemistry, University of California, Riverside, Riverside, California 92521-0403, United States.

Analytical Chemistry
|April 21, 2023
PubMed
Summary

This study reveals how small GTPases, crucial for cell development, change during bone formation in human stem cells. KRAS was identified as a new regulator of osteogenesis, impacting extracellular matrix accumulation.

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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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Area of Science:

  • Cellular Biology
  • Proteomics
  • Stem Cell Differentiation

Background:

  • Small GTPases are vital for cellular processes and early development.
  • Their specific roles in osteogenic differentiation were not well understood.
  • Understanding these roles is key to regenerative medicine and bone biology.

Purpose of the Study:

  • To systematically analyze the small GTPase proteome during osteogenic differentiation of H9 human embryonic stem cells.
  • To identify key small GTPases involved in bone formation.
  • To uncover novel regulators of osteogenesis.

Main Methods:

  • Utilized high-throughput targeted proteomic analysis using scheduled liquid chromatography-multiple-reaction monitoring (LC-MRM).
  • Employed synthetic stable isotope-labeled peptides for accurate quantification.
  • Interrogated temporal changes in the entire small GTPase proteome.

Main Results:

  • The LC-MRM method demonstrated high accuracy, reproducibility, and throughput.
  • Significant alterations in the expression of numerous small GTPases were observed during osteogenic differentiation.
  • A novel role for KRAS in osteogenesis was identified, regulating extracellular matrix accumulation and mineralization by modulating MMP9 activity.

Conclusions:

  • Targeted quantitative proteomics is a powerful tool for studying stem cell differentiation.
  • Osteogenic differentiation involves dynamic changes in the small GTPase proteome, particularly those linked to autophagy.
  • KRAS emerges as a previously unrecognized regulator of osteogenesis, offering new therapeutic targets.