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GTPases and their Regulation

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,...

GTPases and their Regulation

GTPases and their Regulation

What are Viruses?

What are Viruses?

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.

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...

Coat Assembly and GTPases

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...

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Related Experiment Video

Updated: Feb 1, 2026

Modeling Hepatitis B Virus Infection in Non-Hepatic 293T-NE-3NRs Cells

Modeling Hepatitis B Virus Infection in Non-Hepatic 293T-NE-3NRs Cells

Published on: June 5, 2020

Host Cell Rab GTPases in Hepatitis B Virus Infection.

Lisa Zeyen¹, Reinhild Prange¹

¹Department of Virology, University Medical Center of the Johannes Gutenberg University Mainz, Mainz, Germany.

Frontiers in Cell and Developmental Biology

|December 5, 2018

Summary

Hepatitis B virus (HBV) hijacks cellular transport proteins called Rab GTPases for its life cycle. Researchers found Rab7A and Rab33B are key, influencing HBV entry, assembly, and exit.

Keywords:

HBV Rab GAP Rab effector Rab33B Rab7A autophagy virus assembly virus trafficking

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Published on: March 14, 2019

Area of Science:

Virology
Cell Biology
Molecular Biology

Background:

Hepatitis B virus (HBV) infects over 250 million people globally, causing liver disease.
HBV utilizes diverse particle types and host cellular machinery for its propagation.
Understanding HBV's interaction with host pathways is crucial for antiviral strategies.

Purpose of the Study:

To review how HBV exploits and disrupts host Rab GTPase functions.
To focus on the roles of Rab7A and Rab33B in the HBV life cycle.
To explore potential broad-spectrum antiviral targets.

Main Methods:

Review of recent scientific literature on HBV and Rab GTPases.
Analysis of HBV's co-option of host membrane trafficking pathways.
Focus on Rab7A and Rab33B functions in HBV infection.

Main Results:

Rab7A has dual roles: promoting HBV entry and inhibiting virion release.
Rab33B is essential for assembling HBV nucleocapsids, potentially using the Atg5-12/16L1 complex as a scaffold.
HBV manipulates Rab GTPase-directed trafficking for its replication.

Conclusions:

HBV extensively co-opts Rab GTPases, particularly Rab7A and Rab33B, throughout its life cycle.
The Rab33B/Atg5-12/16L1 interaction suggests a novel assembly mechanism exploited by HBV.
Targeting shared Rab-directed pathways could lead to new antiviral therapies for HBV and other viruses.