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Related Concept Videos

Rab Proteins01:14

Rab Proteins

4.6K
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...
4.6K
Rab Cascades01:25

Rab Cascades

3.1K
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.
3.1K

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Related Experiment Video

Updated: Nov 13, 2025

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag

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RBD11, a bioengineered Rab11-binding module for visualizing and analyzing endogenous Rab11.

Futaba Osaki1, Takahide Matsui1, Shu Hiragi1

  • 1Laboratory of Membrane Trafficking Mechanisms, Department of Integrative Life Sciences, Graduate School of Life Sciences, Tohoku University, Aobayama, Aoba-ku, Sendai, Miyagi 980-8578, Japan.

Journal of Cell Science
|March 13, 2021
PubMed
Summary

Researchers engineered RBD11, a Rab11-specific binding domain, to study Rab11 GTPase functions. This tool enables precise visualization and manipulation of Rab11

Keywords:
EffectorMembrane trafficRab11Rab11-binding domainSmall GTPase RabTrapper

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Trafficking

Background:

  • The small GTPase Rab11 (Rab11A and Rab11B) is crucial for membrane protein recycling, cytokinesis, neurite outgrowth, and epithelial morphogenesis.
  • Existing methods using Rab11-binding effector domains, like Rab11-FIP2-C, lack specificity, binding to other Rab proteins (Rab14, Rab25).

Purpose of the Study:

  • To bioengineer a Rab11-specific binding domain for precise analysis of Rab11 function.
  • To develop tools for temporal and reversible analysis of Rab11-dependent membrane trafficking.

Main Methods:

  • Bioengineering of an artificial Rab11-specific binding domain, RBD11.
  • Expression of RBD11 and a tandem construct (2×RBD11) to assess Rab11 localization and function.
  • Development of tetracycline-inducible and FM-tagged RBD11 tools for temporal control.

Main Results:

  • RBD11 expression allowed visualization of endogenous Rab11 without altering its localization or function.
  • Expression of 2×RBD11 inhibited epithelial morphogenesis and caused a multi-lumen phenotype in cysts, indicative of Rab11 deficiency.
  • Development of inducible and tagged tools for controlled study of Rab11-mediated membrane trafficking.

Conclusions:

  • RBD11 is a specific and effective tool for studying Rab11.
  • Engineered tools provide new possibilities for investigating Rab11-dependent cellular processes with temporal and reversible control.