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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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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
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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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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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The Movement of Organelles and Vesicles01:43

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In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
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Updated: Apr 10, 2026

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
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Functional homologies in vesicle tethering.

Anne Kuhlee1, Stefan Raunser1, Christian Ungermann2

  • 1Department of Structural Biochemistry, Max-Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.

FEBS Letters
|June 15, 2015
PubMed
Summary
This summary is machine-generated.

The HOPS complex, a key factor in membrane fusion, requires structural flexibility for its function. Making the HOPS tethering factor more rigid impairs its ability to mediate SNARE-driven membrane fusion.

Keywords:
HOPSProtein complexStructural flexibilityTetheringVesicle

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The HOPS (homotypic vacuole protein sorting) tethering factor is a crucial macromolecular complex involved in membrane fusion.
  • It plays a key role in the fusion of multivesicular bodies and vacuoles, essential cellular processes.

Purpose of the Study:

  • To investigate the role of structural flexibility in the function of the HOPS complex.
  • To compare the HOPS complex with other tethering factors to understand common mechanisms in membrane tethering and fusion.

Main Methods:

  • Electron microscopy was used to study the structural flexibility of the purified HOPS complex.
  • Biochemical modifications were employed to alter the rigidity of the HOPS complex.

Main Results:

  • Electron microscopy revealed inherent structural flexibility within the purified HOPS complex.
  • Increased rigidity of the HOPS complex, induced by biochemical modification, significantly reduced its ability to mediate SNARE-driven membrane fusion.

Conclusions:

  • Structural flexibility is not merely a characteristic but an essential requirement for the functional activity of the HOPS complex in membrane fusion.
  • Understanding the mechanisms of tethering factors like HOPS provides insights into fundamental cellular processes of membrane trafficking and fusion.