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Related Concept Videos

Rab Proteins01:14

Rab Proteins

4.4K
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...
4.4K

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Related Experiment Video

Updated: Oct 22, 2025

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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High-Throughput Assay for Profiling the Substrate Specificity of Rab GTPase-Activating Proteins.

Ashwini K Mishra1, David G Lambright2

  • 1Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|August 28, 2021
PubMed
Summary
This summary is machine-generated.

Researchers developed a sensitive, high-throughput assay to measure GTPase-activating Protein (GAP) activity on Rab GTPases. This new method quantifies inorganic phosphate release, aiding in understanding GAP-GTPase interactions.

Keywords:
GAP assayGAP reactionGTP hydrolysisGTPaseHigh-throughputPBP-MDCCPhosphatePhosphate-binding proteinRab GTPase

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Signaling

Background:

  • GTP hydrolysis by GTPase-activating Proteins (GAPs) is crucial for regulating GTPase function.
  • The Rab GTPase family has over 60 human members, with many putative GAPs identified.
  • Identifying specific Rab GTPase substrates and determining GAP specificity remains a significant challenge.

Purpose of the Study:

  • To develop a sensitive, high-throughput method for profiling GAP activity towards Rab GTPases.
  • To overcome limitations in identifying target substrates and determining specificity within the Rab family.

Main Methods:

  • A microplate-based assay was developed to quantitatively measure GTP hydrolysis.
  • The method detects inorganic phosphate release using a fluorescent phosphate sensor.
  • It requires relatively low protein concentrations and is adaptable to various GAP-GTPase systems.

Main Results:

  • The assay provides a sensitive and high-throughput platform for measuring GAP activity.
  • It enables quantitative profiling of GAP activity across the Rab GTPase family.
  • The method demonstrates broad applicability to different GAP-GTPase interactions.

Conclusions:

  • This novel assay facilitates the characterization of Rab GTPase regulation by GAPs.
  • It offers a valuable tool for discovering and validating GAP-GTPase specificities.
  • The method can advance the understanding of GTPase function in various cellular processes.