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Rab Cascades

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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

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Excitatory and Inhibitory Effects of Neurotransmitters

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Related Experiment Video

Updated: Jul 12, 2026

Presynaptically Silent Synapses Studied with Light Microscopy

Presynaptically Silent Synapses Studied with Light Microscopy

Published on: January 4, 2010

CAST controls presynaptic sequestration of Rab6 in neurons.

Yamato Hida¹, Atsushi Shimada², Yeon-Jeong Kim¹

¹Department of Biochemistry, Graduate School of Medicine/Faculty of Medicine, University of Yamanashi, 1110 Shimokato, Chuo, Yamanashi, 409-3898, Japan.

Molecular Brain

|July 10, 2026

Summary

This summary is machine-generated.

CAST protein directly binds Rab6 GTP, restricting its presynaptic accumulation. This CAST-dependent mechanism spatially organizes Rab6 at presynaptic boutons, crucial for trafficking.

Keywords:

CAST Membrane trafficking Presynaptic bouton Rab GTPase Rab6 Synaptic scaffold proteins

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Related Experiment Videos

Last Updated: Jul 12, 2026

Presynaptically Silent Synapses Studied with Light Microscopy

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Published on: January 4, 2010

An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins

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Published on: June 26, 2018

An Engulfment Assay: A Protocol to Assess Interactions Between CNS Phagocytes and Neurons

An Engulfment Assay: A Protocol to Assess Interactions Between CNS Phagocytes and Neurons

Published on: June 8, 2014

Area of Science:

Neuroscience
Cell Biology
Molecular Biology

Background:

CAST is a key scaffold protein in the active zone.
Its precise function in Rab6-dependent trafficking is not well understood.

Purpose of the Study:

To elucidate the role of CAST in Rab6-dependent trafficking.
To identify the specific CAST domain responsible for Rab6 interaction.

Main Methods:

Biochemical mapping
Isothermal titration calorimetry
Bimolecular fluorescence complementation
Cultured hippocampal neuron imaging

Main Results:

The coiled-coil domain of CAST (CC10) directly binds Rab6-GTP.
CAST selectively interacts with the GTP-bound form of Rab6.
CAST promotes presynaptic accumulation of Rab6 in neurons.
CC10 mutations disrupt Rab6 presynaptic localization.

Conclusions:

CAST acts as a Rab6-binding module, spatially restricting Rab6 at presynaptic boutons.
This defines a CAST-dependent mechanism for Rab6 cargo capture and presynaptic trafficking organization.