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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...

Leaky Scanning

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA. Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...

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.

Small GTPases - Ras and Rho

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:

Regulation of Nuclear Protein Sorting

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...

Types of RNA

Types of RNA

Overview
Three main types of RNA are involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). These RNAs perform diverse functions and can be broadly classified as protein-coding or non-coding RNA. Non-coding RNAs play important roles in the regulation of gene expression in response to developmental and environmental changes. Non-coding RNAs in prokaryotes can be manipulated to develop more effective antibacterial drugs for human or animal use.
RNA...

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Related Experiment Video

Updated: Jun 17, 2026

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Published on: September 30, 2016

RNA-Binding Protein RBM25 Targets the mRNA Stability of GTPase Rab22a to Restrict Viral Entry and Infection.

Yingying Ding^1,2, Huiying Chen¹, Yuyu Jiang¹

¹National Key Laboratory of Immunity & Inflammation, Department of Pathogen Biology, Naval Medical University, Shanghai, China.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)

|June 16, 2026

Summary

The RNA-binding protein RBM25 acts as a broad-spectrum antiviral factor by blocking viral entry, independent of interferon signaling. This discovery reveals a new pathway for developing broad-spectrum antiviral therapies.

Keywords:

RBM25 RC3H1 Rab22a antiviral immunity mRNA stability respiratory virus viral entry

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Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

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Last Updated: Jun 17, 2026

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Novel RNA-Binding Proteins Isolation by the RaPID Methodology

Published on: September 30, 2016

An Assay for Quantifying Protein-RNA Binding in Bacteria

An Assay for Quantifying Protein-RNA Binding in Bacteria

Published on: June 12, 2019

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Spatio-Temporal Manipulation of Small GTPase Activity at Subcellular Level and on Timescale of Seconds in Living Cells

Published on: March 9, 2012

Area of Science:

Virology
Immunology
Molecular Biology

Background:

Viral infections activate complex host defenses, but key regulatory mechanisms are not fully understood.
The type I interferon (IFN-I) pathway is a critical antiviral defense, yet other pathways remain to be elucidated.

Purpose of the Study:

To identify novel host factors that regulate antiviral responses.
To investigate the role of RNA-binding protein RBM25 in host defense against viral infections.
To elucidate the molecular mechanisms underlying RBM25's antiviral activity.

Main Methods:

Investigated RBM25 expression in viral infections.
Assessed viral susceptibility and tissue damage in RBM25-deficient mice.
Performed in vitro studies to evaluate RBM25's effect on viral replication.
Elucidated the interaction of RBM25 with Rab22a and RC3H1 using post-transcriptional analysis.

Main Results:

RBM25 acts as a potent, broad-spectrum antiviral factor, inhibiting RNA and DNA viruses independently of IFN-I.
Viral infections downregulate RBM25, leading to increased susceptibility and tissue damage.
RBM25 suppresses viral entry by downregulating the host GTPase Rab22a.
RBM25, with RC3H1, destabilizes Rab22a mRNA, limiting its translation and viral entry.

Conclusions:

The RBM25/RC3H1-Rab22a axis represents an interferon-independent pathway controlling viral entry via mRNA stability.
RBM25 is a crucial host antiviral factor that targets an early step in the viral life cycle.
This pathway offers a potential target for developing novel broad-spectrum antiviral strategies.