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Related Concept Videos

GTPases and their Regulation02:14

GTPases and their Regulation

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, also known...
Rab Proteins01:14

Rab Proteins

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...
GTPases and their Regulation02:14

GTPases and their Regulation

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, also known...
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

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:
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

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...
Transducer Mechanism: G Protein–Coupled Receptors01:30

Transducer Mechanism: G Protein–Coupled Receptors

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.
GPCRs are also called heptahelical, 7TM, or...

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Related Experiment Video

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Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

Comparing the Affinity of GTPase-binding Proteins using Competition Assays

Published on: October 8, 2015

DRG: a novel developmentally regulated GTP-binding protein.

T Sazuka1, Y Tomooka, Y Ikawa

  • 1Laboratory of Molecular Oncology, RIKEN, Tsukuba Life Science Center, Ibaraki, Japan.

Biochemical and Biophysical Research Communications
|November 30, 1992
PubMed
Summary

Researchers identified a novel GTP-binding protein, named DRG, crucial for embryonic brain development. This evolutionarily conserved protein, found across species, plays a key role in cell physiology.

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Last Updated: Jul 10, 2026

Comparing the Affinity of GTPase-binding Proteins using Competition Assays
10:37

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Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
13:51

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Published on: November 11, 2018

Identifying the Binding Proteins of Small Ligands with the Differential Radial Capillary Action of Ligand Assay (DRaCALA)
09:26

Identifying the Binding Proteins of Small Ligands with the Differential Radial Capillary Action of Ligand Assay (DRaCALA)

Published on: March 19, 2021

Area of Science:

  • Molecular Biology
  • Developmental Biology
  • Biochemistry

Background:

  • Previously isolated murine cDNA clones expressed in the embryonic brain and down-regulated during development.
  • Focus on identifying novel genes involved in developmental processes.

Purpose of the Study:

  • To characterize a novel GTP-binding protein identified from embryonic brain cDNA library.
  • To investigate the evolutionary conservation and functional role of the novel protein.

Main Methods:

  • Subtraction cloning approach to isolate differentially expressed genes.
  • Bioinformatic analysis to predict protein structure and identify conserved motifs.
  • In vitro GTP-binding assays using bacterially expressed and cellular DRG proteins.

Main Results:

  • One cDNA clone encodes a novel 40.5 kD GTP-binding protein, designated DRG.
  • DRG protein possesses five characteristic GTP-binding protein structural motifs.
  • Both bacterially expressed and endogenous DRG proteins bind GTP in vitro.
  • Homologous sequences to DRG are present in diverse species like Drosophila and Halobacterium.

Conclusions:

  • DRG represents a novel, evolutionarily conserved class of GTP-binding proteins.
  • The DRG protein likely plays a significant role in fundamental cell physiology.
  • Further research is warranted to elucidate the specific functions of DRG in development and other cellular processes.