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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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Updated: Feb 23, 2026

Induction of Protein Deletion Through In Utero Electroporation to Define Deficits in Neuronal Migration in Transgenic Models

Induction of Protein Deletion Through In Utero Electroporation to Define Deficits in Neuronal Migration in Transgenic Models

Published on: January 12, 2015

WDR91 is a Rab7 effector required for neuronal development.

Kai Liu^1,2, Ruxiao Xing^1,3, Youli Jian¹

¹State Key Laboratory of Molecular and Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.

The Journal of Cell Biology

|September 2, 2017

Summary

This summary is machine-generated.

The WD40-repeat protein WDR91 is crucial for endosome conversion, acting as a Rab7 effector. Its absence disrupts endosomal-lysosomal trafficking and impairs neuronal development, leading to severe phenotypes.

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Area of Science:

Cell Biology
Molecular Biology
Neuroscience

Background:

Endosome-to-lysosome trafficking is vital for cellular function.
This process requires precise molecular switches, including Rab GTPases and phosphoinositides.
Dysregulation of endosomal trafficking is implicated in various diseases.

Purpose of the Study:

To identify novel proteins involved in the Rab5-to-Rab7 switch during endosome maturation.
To elucidate the function of WDR91 in the endosomal-lysosomal pathway.
To investigate the role of WDR91 in neuronal development and survival.

Main Methods:

Yeast two-hybrid screening to identify Rab7-interacting proteins.
Biochemical assays to determine WDR91's effect on phosphoinositide levels and kinase activity.
Generation and analysis of Wdr91 knockout and conditional knockout mouse models.
Primary neuronal culture and imaging to assess neuronal morphology and trafficking.

Main Results:

WDR91 was identified as a Rab7 effector that promotes the transition from early to late endosomes.
Loss of WDR91 leads to elevated PtdIns3P levels, endosome maturation arrest, and blocked lysosomal delivery.
Global Wdr91 knockout causes neonatal lethality; brain-specific inactivation results in severe neurodevelopmental defects and postnatal death.
WDR91 deficiency in neurons causes enlarged endosomes and impaired neurite outgrowth, phenotypes rescued by functional WDR91.

Conclusions:

WDR91 is an essential Rab7 effector that regulates phosphoinositide dynamics during endosome conversion.
WDR91 plays a critical role in the endosomal-lysosomal pathway and is indispensable for normal brain development and neuronal function.