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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...
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Rab Cascades01:25

Rab Cascades

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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.
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Related Experiment Video

Updated: Oct 22, 2025

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag

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Detecting Endogenous Rab8 Activation.

Samuel J Tong1, Richard M Lucas1, Zhijian Xiao1

  • 1Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, Australia.

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

Researchers developed novel molecular probes to measure the activation of Rab GTPases (guanosine triphosphateases) in cells. The OCRL-RBD probe efficiently captures active GTP-bound Rab8, aiding cellular signaling research.

Keywords:
GDPGTPGTPaseNucleotide exchangeOCRLPI3KγRab activationRab8

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Rab GTPases are key regulators of intracellular trafficking and signaling pathways.
  • Their activity is controlled by a GDP/GTP switch, making GTP-bound state an indicator of activation.
  • Current methods for assessing endogenous Rab activation in cells are limited.

Purpose of the Study:

  • To develop and validate molecular probes for detecting endogenous GTP-bound Rab8.
  • To assess Rab8 activation in response to lipopolysaccharide (LPS) in mouse macrophages.
  • To compare the efficiency of probes derived from Rab8 effectors OCRL and PI3Kγ.

Main Methods:

  • Development of molecular probes based on Rab effector domains (OCRL-RBD and PI3Kγ-RBD).
  • Utilizing these probes for pull-down assays to capture GTP-bound Rab8 from cell extracts.
  • Employing LPS stimulation in mouse macrophages as a model system for Rab8 activation.

Main Results:

  • Two molecular probes were successfully developed to detect GTP-bound Rab8.
  • The OCRL-RBD probe demonstrated higher efficiency in capturing GTP-bound Rab8 compared to the PI3Kγ-RBD probe.
  • The method effectively assessed LPS-induced Rab8 activation in mouse macrophages.

Conclusions:

  • The OCRL-RBD probe provides an efficient means to measure endogenous Rab8 activation.
  • This method is applicable to various cell and tissue extracts for studying GTP-bound Rab8.
  • The developed probes advance the study of Rab GTPase function in cellular processes.