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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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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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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...
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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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Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
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Related Experiment Video

Updated: Sep 17, 2025

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
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Flippase-Mediated Hybrid Vesicle Division.

Paula De Dios Andres1, Amalie Benfeldt Purup1,2, Grégory Beaune3

  • 1Interdisciplinary Nanoscience Center (iNANO), Aarhus University, Aarhus, 8000, Denmark.

Advanced Materials (Deerfield Beach, Fla.)
|July 4, 2025
PubMed
Summary
This summary is machine-generated.

Researchers created synthetic vesicles that divide like cells using a protein-mediated lipid flippase. The hydrophobic block copolymers in hybrid vesicles are key to this cell division process.

Keywords:
hybrid vesiclelipid flippasemembrane constrictiontransmembrane asymmetryvesicle division

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Area of Science:

  • Synthetic biology
  • Biophysics
  • Cellular mechanics

Background:

  • Protein-mediated cell division is a complex process that is challenging to replicate in synthetic systems.
  • Bottom-up synthetic biology aims to construct artificial cellular systems with life-like functions.

Purpose of the Study:

  • To reconstitute an active lipid flippase (Drs2p-Cdc50p) within polymer lipid hybrid vesicles (HVs).
  • To investigate the role of amphiphilic block copolymers in facilitating protein-mediated vesicle division.

Main Methods:

  • Assembly of HVs using phospholipids and amphiphilic block copolymers with varying hydrophobic blocks.
  • Reconstitution of Drs2p-Cdc50p within HVs to induce lipid translocation.
  • Analysis of vesicle constriction and division dynamics.

Main Results:

  • Successful reconstitution of active Drs2p-Cdc50p in HVs, leading to lipid asymmetry.
  • Demonstrated that the hydrophobic block's chemical nature is critical for supporting bilayer curvature changes.
  • Observed vesicle constriction and division driven by lipid translocation.

Conclusions:

  • The chemical properties of hydrophobic blocks in amphiphilic block copolymers are essential for protein-mediated vesicle division.
  • This work represents a significant advance in mimicking cell division in synthetic assemblies.
  • Potential for developing bottom-up assembled self-replicating units.