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Related Concept Videos

Rab Proteins01:14

Rab Proteins

5.5K
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...
5.5K
Rab Cascades01:25

Rab Cascades

3.8K
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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Related Experiment Video

Updated: Apr 21, 2026

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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Characterization of Rabaptin-5 γ isoform.

E V Korobko1, S L Kiselev, I V Korobko

  • 1Institute of Gene Biology, Russian Academy of Sciences, Moscow, 119334, Russia. igorvk@igb.ac.ru.

Biochemistry. Biokhimiia
|November 12, 2014
PubMed
Summary

Alternative splicing generates Rabaptin-5 isoforms with distinct functions. Rabaptin-5γ, an isoform, localizes to the trans-Golgi network, not early endosomes, indicating a role beyond Rab5-mediated transport.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Membrane Trafficking

Background:

  • Rab GTPases regulate intracellular membrane traffic via effector proteins.
  • Rabaptin-5, a Rab5 effector, links early endosomes and Rab4 compartments.
  • Alternative splicing produces Rabaptin-5 isoforms with potentially different functions.

Purpose of the Study:

  • To investigate the function and localization of the Rabaptin-5γ isoform.
  • To understand the impact of alternative splicing on Rab effector protein activity.

Main Methods:

  • Immunofluorescence microscopy to determine protein localization.
  • Co-immunoprecipitation assays to study protein interactions.
  • Analysis of Rabaptin-5γ expression and localization in cellular compartments.

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Last Updated: Apr 21, 2026

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
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Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

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Main Results:

  • Rabaptin-5γ interacts with Rab5 but is not found on early endosomes.
  • Endogenous Rabaptin-5γ predominantly localizes to the trans-Golgi network.
  • Rabaptin-5γ is also found in Rab4-positive compartments, suggesting a role in later trafficking steps.

Conclusions:

  • Rabaptin-5γ's localization indicates it functions in post-early endosome trafficking pathways.
  • Alternative splicing of Rabaptin-5 generates functional diversity in Rab effector proteins.
  • This diversity allows for specialized roles in intricate membrane transport networks.