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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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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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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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Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients
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Self-limiting aggregation of phospholipid vesicles.

N de Lange1, F A M Leermakers1, J M Kleijn1

  • 1Physical Chemistry & Soft Matter, Wageningen University and Research, Stippeneng 4, 6708 WE, Wageningen, The Netherlands. frans.leermakers@wur.nl.

Soft Matter
|February 18, 2020
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Summary
This summary is machine-generated.

Researchers developed three methods to create stable vesicle pairs for studying membrane interactions. One method uses temperature-sensitive polymers for reversible aggregation, maintaining vesicle integrity.

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Area of Science:

  • Biophysics
  • Materials Science
  • Colloid Science

Background:

  • Lipid vesicles are crucial model systems for biological membrane research.
  • Studying self-assembled vesicle pairs offers insights into membrane interactions.
  • Achieving stable vesicle pairs while maintaining colloidal stability is a significant challenge.

Purpose of the Study:

  • To develop and assess strategies for forming stable, finite-sized aggregates of phospholipid vesicles.
  • To investigate the mechanisms and conditions for vesicle pair formation and stability.
  • To explore reversible aggregation using temperature-sensitive polymers.

Main Methods:

  • Utilized biotinylated lipids and streptavidin for vesicle coupling.
  • Employed bridging attraction with cationic polymers (polylysine) for negatively charged vesicles.
  • Investigated temperature-induced aggregation using vesicles and a thermo-sensitive surfactant (pNIPAm).
  • Assessed aggregate formation and stability using dynamic light scattering, static light scattering, and fluorescence correlation spectroscopy.

Main Results:

  • Successfully demonstrated three distinct strategies for creating stable vesicle aggregates.
  • Identified temperature-responsive aggregation using pNIPAm, enabling reversible vesicle pairing above the Lower Critical Solution Temperature (LCST).
  • Confirmed that individual vesicles maintain structural integrity (no fusion or leakage) within the formed vesicle pairs.
  • Characterized aggregate size distributions under various conditions.

Conclusions:

  • Developed robust methods for stable vesicle pair formation, crucial for membrane interaction studies.
  • The temperature-controlled aggregation strategy offers reversible control over vesicle assembly.
  • The findings indicate that vesicle pairs can be formed and maintained without compromising individual vesicle integrity.