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Related Concept Videos

Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...

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Related Experiment Video

Updated: May 18, 2026

Image-Based Methods to Study Membrane Trafficking Events in Stomatal Lineage Cells
11:31

Image-Based Methods to Study Membrane Trafficking Events in Stomatal Lineage Cells

Published on: May 12, 2023

LRRK2 and vesicle trafficking.

Giovanna Sanna1, Maria Grazia Del Giudice, Claudia Crosio

  • 1Department of Biomedical Sciences, University of Sassari, Sassari, Italy.

Biochemical Society Transactions
|September 20, 2012
PubMed
Summary

Mutations in leucine-rich repeat kinase 2 (LRRK2) are a significant genetic cause of Parkinson's disease. This review explores LRRK2's role in regulating membrane trafficking, a process crucial for neuronal function.

Area of Science:

  • Neuroscience
  • Genetics
  • Cell Biology

Background:

  • Mutations in leucine-rich repeat kinase 2 (LRRK2), also known as PARK8 or dardarin, cause autosomal-dominant Parkinson's disease (PD).
  • LRRK2 mutations are a major genetic risk factor for familial and sporadic PD, particularly in specific populations.
  • The precise pathophysiological role of LRRK2 in PD remains unclear despite extensive research.

Purpose of the Study:

  • To review recent evidence on the potential function of LRRK2 in membrane trafficking.
  • To elucidate the role of LRRK2 in cellular processes relevant to Parkinson's disease.

Main Methods:

  • Literature review of recent studies on LRRK2 function.
  • Analysis of evidence linking LRRK2 to membrane trafficking pathways.

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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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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

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Related Experiment Videos

Last Updated: May 18, 2026

Image-Based Methods to Study Membrane Trafficking Events in Stomatal Lineage Cells
11:31

Image-Based Methods to Study Membrane Trafficking Events in Stomatal Lineage Cells

Published on: May 12, 2023

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
08:55

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

Published on: December 14, 2017

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
08:55

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

Published on: December 29, 2017

Main Results:

  • LRRK2 may play a role in regulating membrane trafficking.
  • This regulation spans from vesicle generation and cytoskeletal movement to vesicle fusion.

Conclusions:

  • LRRK2's involvement in membrane trafficking offers a potential explanation for its role in Parkinson's disease pathogenesis.
  • Further research into LRRK2's function in membrane trafficking is warranted to understand PD onset and progression.