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Related Concept Videos

Clathrin Coated Vesicles01:12

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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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Coat Assembly and GTPases01:33

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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...
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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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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.
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Protein Transport to the Thylakoids01:22

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Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
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Cotranslational Protein Translocation01:20

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
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Pinching-off of Coated Vesicles01:32

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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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Atg27p localization is clathrin- and Ent3p/5p-dependent.

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The autophagy protein Atg27p localizes to specific cellular structures. Its localization depends on clathrin and the Ent3p/5p adaptors, revealing new insights into cellular transport mechanisms.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Autophagy Research

Background:

  • The autophagy-related protein Atg27p is known to localize to the pre-autophagosomal structure (PAS) and various organelles, including the late Golgi, vacuolar membrane, and endosome.
  • Atg27p's vacuolar membrane localization is linked to its C-terminal tyrosine sorting motif and the AP-3 adaptor.
  • Previous observations indicate Atg27p can be present in clathrin-coated vesicles.

Purpose of the Study:

  • To investigate the role of clathrin and its associated cargo adaptors in the cellular localization of Atg27p.
  • To determine if Atg27p's intracellular trafficking is mediated by clathrin-dependent pathways.

Main Methods:

  • Analysis of Atg27p localization in yeast cells under conditions affecting clathrin and adaptor protein function.
  • Utilizing genetic and cell biological techniques to assess the dependency of Atg27p localization on clathrin and specific adaptors like Ent3p/5p.

Main Results:

  • Atg27p's localization within the cell is dependent on the presence and function of clathrin.
  • The study identified a specific dependency of Atg27p localization on the cargo adaptors Ent3p and Ent5p (Ent3p/5p).

Conclusions:

  • Cellular localization of Atg27p is regulated by clathrin-mediated trafficking pathways.
  • Ent3p/5p adaptors play a crucial role in directing Atg27p to its correct cellular compartments, likely via clathrin-coated vesicles.