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Overview of Secretory Vesicles01:33

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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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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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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Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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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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Related Experiment Video

Updated: May 5, 2026

Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients
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Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients

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Dynamin undergoes a GTP-dependent conformational change causing vesiculation

S M Sweitzer1, J E Hinshaw

  • 1Laboratory of Cell Biochemistry and Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.

Cell
|July 11, 1998
PubMed
Summary
This summary is machine-generated.

Dynamin, a GTPase, acts as a mechanochemical enzyme essential for vesicle formation. Purified dynamin alone can constrict and form vesicles from lipid bilayers upon GTP addition, supporting its role in membrane fission.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Dynamin GTPases are crucial for endocytosis and synaptic vesicle recycling.
  • Dynamin's role in vesicle formation from the trans-Golgi network is a recent discovery.
  • Dynamin is hypothesized to assemble around clathrin-coated pits to aid vesicle pinching.

Purpose of the Study:

  • To investigate dynamin's mechanochemical properties.
  • To determine if dynamin alone can drive membrane fission.
  • To support the hypothesis of dynamin as the force-generating molecule in membrane fission.

Main Methods:

  • Purification of recombinant dynamin.
  • Binding of dynamin to lipid bilayers.
  • Observation of dynamin-lipid interactions using electron microscopy (implied).
  • GTP addition to induce conformational changes and vesicle formation.

Main Results:

  • Purified recombinant dynamin self-assembles on lipid bilayers into helical tubes.
  • GTP addition causes constriction and vesiculation of these dynamin-lipid structures.
  • Dynamin alone demonstrates the ability to form constricted necks.

Conclusions:

  • Dynamin functions as a mechanochemical enzyme.
  • Dynamin is sufficient for generating the forces required for membrane fission.
  • These findings support dynamin's unique role in vesicle formation and membrane scission.