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Related Concept Videos

Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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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...
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Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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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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COP Coated Vesicles00:59

COP Coated Vesicles

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Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
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Delivery Pathways to the Lysosome01:36

Delivery Pathways to the Lysosome

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Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
Endocytosis
In endocytosis, the cell membrane takes up macromolecules and particles from the surrounding medium. Clathrin-mediated...
10.4K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.6K
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...
4.6K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

3.3K
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...
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Related Experiment Video

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In vivo and in vitro Studies of Adaptor-clathrin Interaction
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In vivo and in vitro Studies of Adaptor-clathrin Interaction

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Clathrin localization and dynamics in Aspergillus nidulans.

Z Schultzhaus1, T B Johnson1, B D Shaw1

  • 1Department of Plant Pathology and Microbiology, Texas A&M University, 2132 TAMU, College Station, TX, 77845, USA.

Molecular Microbiology
|October 15, 2016
PubMed
Summary

Clathrin is essential for filamentous fungal growth, localizing to the Golgi and moving puncta, but not significantly involved in endocytosis in Aspergillus nidulans.

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Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
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Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
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Area of Science:

  • Cell Biology
  • Mycology

Background:

  • Cell growth requires membrane remodeling, regulated by coat proteins like clathrin.
  • Filamentous fungi concentrate exocytosis and endocytosis at their hyphal tips.

Purpose of the Study:

  • To investigate the role of clathrin heavy chain (ClaH) in membrane remodeling during hyphal growth in Aspergillus nidulans.

Main Methods:

  • Examined localization of clathrin heavy chain fused with GFP (ClaH-GFP).
  • Observed colocalization with late Golgi and endocytic markers.
  • Assessed clathrin's role in growth and endocytosis via FM4-64 internalization and gene repression.

Main Results:

  • ClaH-GFP localized to late Golgi, the endocytic collar, and mobile puncta.
  • Clathrin hubs dispersed after a late Golgi marker.
  • Clathrin was essential for growth but did not significantly participate in endocytosis.

Conclusions:

  • Clathrin plays a vital role in hyphal growth in Aspergillus nidulans.
  • Clathrin's primary function is likely not in endocytosis in this organism.
  • ClaH puncta exhibit movement distinct from early endosomes.