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Related Concept Videos

GTPases and their Regulation02:14

GTPases and their Regulation

9.6K
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.
Large G-proteins,...
9.6K
GTPases and their Regulation02:14

GTPases and their Regulation

2.7K
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Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

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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.
Three regulatory proteins control their activity:
5.1K
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

10.5K
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...
10.5K
Rab Proteins01:14

Rab Proteins

4.9K
Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
4.9K
Rab Cascades01:25

Rab Cascades

3.3K
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
3.3K

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Related Experiment Video

Updated: Dec 27, 2025

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

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Small GTPases: Structure, biological function and its interaction with nanoparticles.

Siyang Song1,2, Wenshu Cong2, Shurong Zhou2

  • 1Shenyang Pharmaceutical University, No. 103, Wenhua Road, Shenyang 110016, China.

Asian Journal of Pharmaceutical Sciences
|February 28, 2020
PubMed
Summary
This summary is machine-generated.

This review explores small GTPases and their interactions with nanoparticles for nanomedicine. Understanding this interplay is crucial for developing novel therapeutic strategies targeting GTPases.

Keywords:
NanoparticlesRabRasRhoSmall GTPase

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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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Analyzing the Function of Small GTPases by Microinjection of Plasmids into Polarized Epithelial Cells
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Comparing the Affinity of GTPase-binding Proteins using Competition Assays
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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
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Analyzing the Function of Small GTPases by Microinjection of Plasmids into Polarized Epithelial Cells
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Area of Science:

  • Biochemistry
  • Cell Biology
  • Nanotechnology

Background:

  • Small GTPases are essential GTP-binding proteins regulating critical cellular processes like cytoskeletal organization and cell cycle progression.
  • The interaction between GTPases and nanoparticles is increasingly relevant due to the growing use of nanomedicine in biomedical applications.
  • A comprehensive review on GTPase-nanoparticle interactions is currently lacking.

Purpose of the Study:

  • To review the structure, biological functions, and nanoparticle interactions of small GTPases.
  • To introduce various nanoparticles (e.g., gold/silver nanoparticles, SWCNT, polymeric micelles) that interact with GTPases.
  • To highlight the significance of GTPase-nanoparticle interplay for future nanomedicine development.

Main Methods:

  • Literature review of existing studies on small GTPases and nanoparticle interactions.
  • Summary of nanoparticle types and their mechanisms of action with GTPases.
  • Analysis of therapeutic strategies and design concepts in GTPase-targeted nanomedicine.

Main Results:

  • Small GTPases are vital regulators of numerous cellular functions.
  • Diverse nanoparticles interact with GTPases, exhibiting varied pharmacological effects and targeting strategies.
  • Current research indicates potential for nanomedicine to modulate GTPase activity.

Conclusions:

  • Targeting small GTPases with nanomedicine represents a promising new research direction.
  • Understanding GTPase functional mechanisms can guide the design of advanced nanomedicines.
  • Further investigation into GTPase-nanoparticle interactions is essential for therapeutic innovation.