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Related Concept Videos

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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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.
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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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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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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
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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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Related Experiment Video

Updated: Sep 7, 2025

Purification of Extracellular Trypanosomes, Including African, from Blood by Anion-Exchangers Diethylaminoethyl-cellulose Columns
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Stage-Specific COPII-Mediated Cargo Selectivity in African Trypanosomes.

Mohamed Sharif1, James D Bangs2

  • 1Department of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, Buffalo, New York, USA.

Msphere
|June 21, 2022
PubMed
Summary
This summary is machine-generated.

African trypanosomes alter their COPII vesicle transport machinery between life stages. Selectivity for GPI-anchored protein export is lost in insect stage parasites, impacting protein trafficking.

Keywords:
COPIIER exitglycosylphosphatidylinositoltrypanosomevariant surface glycoprotein

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Parasitology

Background:

  • Eukaryotic cells utilize a secretory pathway for intracellular transport, with COPII-coated vesicles mediating ER to Golgi transport.
  • African trypanosomes possess stage-specific secretory pathways crucial for their parasitic life cycle and surface coat synthesis.

Purpose of the Study:

  • To investigate the functional differences in COPII vesicle coat complex assembly and cargo selectivity between bloodstream and insect stages of African trypanosomes.
  • To determine the essentiality and specific roles of Sec23/24 paralogs in COPII transport in procyclic insect-form trypanosomes.

Main Methods:

  • RNA interference (RNAi) knockdowns were employed to assess the essentiality of TbSec23 and TbSec24 isoforms in procyclic trypanosomes.
  • Analysis of cargo trafficking, including glycosylphosphatidylinositol-anchored proteins (GPI-APs) and lysosomal proteins, following RNAi silencing.

Main Results:

  • All TbSec23 and TbSec24 isoforms are essential for procyclic trypanosome survival.
  • Loss of cargo selectivity for GPI-APs was observed in insect-stage parasites compared to bloodstream-stage parasites.
  • Silencing of the TbSec23.2/TbSec24.1 heterodimer significantly impacted the trafficking of soluble proteins like TbCatL.

Conclusions:

  • COPII-mediated transport selectivity is altered between bloodstream and insect stages of African trypanosomes, suggesting adaptation to their digenetic life cycle.
  • These findings highlight stage-specific adaptations in the secretory pathway of African trypanosomes, impacting surface protein dynamics and host-parasite interactions.