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Rab Proteins

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...

Rab Cascades

Rab Cascades

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: Nov 8, 2025

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

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

Published on: December 14, 2017

SopD from Salmonella specifically inactivates Rab8.

Sergey Savitskiy¹, Aymelt Itzen²

¹Institute of Biochemistry and Signal Transduction, University Medical Centre Hamburg-Eppendorf (UKE), Martinistrasse 52, 20246 Hamburg, Germany; Center for Integrated Protein Science Munich (CIPSM), Department Chemistry, Technical University of Munich, Lichtenbergstrasse 4, 85748 Garching, Germany.

Biochimica Et Biophysica Acta. Proteins and Proteomics

|April 19, 2021

Summary

Salmonella SopD and SopD2 proteins function as GTPase activating proteins (GAPs). These bacterial GAPs inactivate host Rab signaling pathways, impacting Salmonella infection and virulence.

Keywords:

Bacterial effector GTPase activating protein Rab.protein Salmonella

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A Non-Coding Small RNA MicC Contributes to Virulence in Outer Membrane Proteins in Salmonella Enteritidis

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Published on: January 27, 2021

Related Experiment Videos

Last Updated: Nov 8, 2025

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

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Published on: December 14, 2017

Author Spotlight: Efficiently Eliminating Bacteriophages from Infected Salmonella Cultures Using Lipopolysaccharides

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Published on: June 28, 2024

A Non-Coding Small RNA MicC Contributes to Virulence in Outer Membrane Proteins in Salmonella Enteritidis

A Non-Coding Small RNA MicC Contributes to Virulence in Outer Membrane Proteins in Salmonella Enteritidis

Published on: January 27, 2021

Area of Science:

Microbiology
Molecular Biology
Cell Biology

Background:

Salmonella outer protein D (SopD) is a key virulence factor secreted during infection.
SopD homolog SopD2 also exhibits GTPase activating protein (GAP) activity, specifically towards Rab32.

Purpose of the Study:

To identify host Rab-proteins targeted by SopD.
To characterize the substrate specificities and catalytic efficiencies of SopD and SopD2 as RabGAPs.
To elucidate the molecular mechanisms underlying SopD- and SopD2-mediated Rab inactivation.

Main Methods:

Yeast two-hybrid screening to identify SopD-interacting Rab-proteins.
In vitro biochemical assays to determine substrate specificity and catalytic efficiency.
Site-directed mutagenesis to investigate key residues in Rab-protein and GAP interactions.

Main Results:

Rab8a was identified as an exclusive substrate for SopD.
SopD2 demonstrated broader specificity, targeting Rab29, Rab32, and Rab38 in vitro.
Catalytic efficiencies for SopD and SopD2 towards their respective substrates were quantified.
Mutagenesis studies provided insights into the interaction interface between GAPs and Rabs.

Conclusions:

Salmonella SopD and SopD2 function as RabGAPs, inactivating host Rab signaling.
Differential substrate specificities of SopD and SopD2 suggest distinct roles in Salmonella pathogenesis.
Understanding these interactions offers potential targets for therapeutic intervention against Salmonella infections.