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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.

GPI Anchoring of Proteins in the ER Membrane

GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...

Tail-anchoring of Proteins in the ER Membrane

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...

Insertion of Single-pass Transmembrane Proteins in the RER

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...

Post-translational Translocation of Proteins to the RER

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

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Related Experiment Video

Updated: Mar 3, 2026

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein

Published on: June 16, 2023

Membrane localization and dynamics of geranylgeranylated Rab5 hypervariable region.

Eileen Edler¹, Eric Schulze², Matthias Stein¹

¹Molecular Simulations and Design Group, Max Planck Institute for Dynamics of Complex Technical Systems, Sandtorstrasse 1, 39106 Magdeburg, Germany.

Biochimica Et Biophysica Acta. Biomembranes

|April 30, 2017

Summary

Rab5

Keywords:

Hypervariable region Lipid enrichment Lipid-protein interactions Molecular dynamics Peripheral membrane protein Small GTPase

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Area of Science:

Cell Biology
Molecular Biology
Biophysics

Background:

Rab5 GTPase regulates endosomal trafficking and early endosome formation.
The Rab5 C-terminal hypervariable region (HVR) requires geranylgeranyl anchors for membrane association.
The HVR's structural role in protein-membrane recruitment remains unclear due to its flexibility.

Purpose of the Study:

To investigate the structural role of the Rab5 HVR in protein-early endosome membrane recruitment.
To elucidate the initial molecular interactions driving Rab5 to the early endosome membrane.

Main Methods:

Full-atomistic and coarse-grained molecular dynamics simulations.
Simulations performed on the Rab5 HVR (residues 206-215) in three distinct model membranes.
Analysis of electrostatic interactions and free energy changes for membrane extraction.

Main Results:

Specific electrostatic interactions were identified between Rab5 HVR (Arg209) and phosphatidylinositol 3-phosphate (PI(3)P).
PI(3)P acts as a crucial initial contact site for Rab5 recruitment to the early endosome.
Membrane-bound PI(3)P actively recruits to the HVR, promoting Rab5-PI(3)P signaling platforms.

Conclusions:

The Rab5 HVR utilizes electrostatic interactions with PI(3)P for initial membrane targeting.
PI(3)P is a key determinant for recruiting Rab5 to early endosomes, facilitating signaling platform formation.
Molecular dynamics simulations provide structural insights into Rab5-membrane interactions.