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Related Concept Videos

Rab Cascades01:25

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.
Rab Proteins01:14

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...
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR activation may...
Introduction to Membrane Traffic01:44

Introduction to Membrane Traffic

The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
Introduction to Membrane Traffic01:44

Introduction to Membrane Traffic

The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
Recycling Endosomes and Transcytosis00:58

Recycling Endosomes and Transcytosis

The recycling endosome, also known as the endosomal recycling compartment (ERC), is a part of the slow-recycling process of the endocytic pathway. Molecules internalized through receptor-mediated endocytosis are either degraded in the lysosomes or are recycled to the plasma membrane through the fast- or slow-recycling route.
The recycling endosome is not a single organelle but an extensively tubulated network of recycling pathways. It functions in storing molecules or transporting them across...

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Related Experiment Video

Updated: Jul 2, 2026

Viral Tracing of Genetically Defined Neural Circuitry
13:06

Viral Tracing of Genetically Defined Neural Circuitry

Published on: October 17, 2012

Internalized Kv1.5 traffics via Rab-dependent pathways.

Alireza Dehghani Zadeh1, Hongjian Xu, Matthew E Loewen

  • 1Department of Anaesthesiology, Pharmacology and Therapeutics, University of British Columbia, Vancouver, British Columbia, Canada.

The Journal of Physiology
|August 30, 2008
PubMed
Summary
This summary is machine-generated.

Voltage-gated potassium channels like Kv1.5 internalize and quickly recycle. Rab GTPases dynamically regulate Kv1.5 trafficking and functional expression, offering targets for cellular modulation.

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Brain Slice Biotinylation: An Ex Vivo Approach to Measure Region-specific Plasma Membrane Protein Trafficking in Adult Neurons
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Brain Slice Biotinylation: An Ex Vivo Approach to Measure Region-specific Plasma Membrane Protein Trafficking in Adult Neurons

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Last Updated: Jul 2, 2026

Viral Tracing of Genetically Defined Neural Circuitry
13:06

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Published on: October 17, 2012

Brain Slice Biotinylation: An Ex Vivo Approach to Measure Region-specific Plasma Membrane Protein Trafficking in Adult Neurons
06:18

Brain Slice Biotinylation: An Ex Vivo Approach to Measure Region-specific Plasma Membrane Protein Trafficking in Adult Neurons

Published on: April 3, 2014

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Ion Channel Physiology

Background:

  • Postinternalization trafficking of voltage-gated potassium channels remains poorly understood.
  • Kv1.5 channels are crucial for cardiac function and electrical excitability.

Purpose of the Study:

  • To elucidate the postinternalization trafficking pathways of Kv1.5 channels.
  • To investigate the role of Rab GTPases in regulating Kv1.5 channel surface expression.

Main Methods:

  • Utilized cell lines (HEK293 and cardiac myoblasts) and surface labeling techniques.
  • Employed colocalization studies with Rab GTPase markers (Rab4, Rab5, Rab7, Rab11).
  • Assessed functional Kv1.5 expression using dominant-negative Rab constructs and electrophysiology.

Main Results:

  • Kv1.5 channels internalize and rapidly recycle via Rab5/Rab4-positive endosomes.
  • A fraction of internalized Kv1.5 channels are targeted for degradation via Rab7.
  • Inhibition of Rab GTPases (Rab5, Rab4, Rab7, Rab11) significantly increased functional Kv1.5 expression.

Conclusions:

  • Kv1.5 trafficking is dynamically regulated by Rab GTPases, influencing surface expression levels.
  • Rab GTPases represent key targets for modulating Kv1.5 channel activity in cells.
  • Understanding these pathways is critical for targeting Kv1.5 channel function in physiological and pathological contexts.