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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 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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Video Experimental Relacionado

Updated: May 5, 2026

Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients
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La dinamina sufre un cambio conformacional dependiente de GTP que causa la vesiculación.

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
Resumen

La dinamina, una GTPasa, actúa como una enzima mecanoquímica esencial para la formación de vesículas. La dinamina purificada sola puede constreñirse y formar vesículas de las bicapas lipídicas tras la adición de GTP, apoyando su papel en la fisión de la membrana.

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Área de la Ciencia:

  • Biología Molecular Biología Molecular
  • Biología celular Biología celular.
  • La bioquímica es la bioquímica.

Sus antecedentes:

  • Las dinamina GTPasas son cruciales para la endocitosis y el reciclaje de las vesículas sinápticas.
  • El papel de la dinamina en la formación de vesículas de la red trans-Golgi es un descubrimiento reciente.
  • Se supone que la dinamina se reúne alrededor de los hoyos recubiertos de clatrina para ayudar a pellizcar las vesículas.

Objetivo del estudio:

  • Para investigar las propiedades mecanoquímicas de la dinamina.
  • Para determinar si la dinamina por sí sola puede impulsar la fisión de la membrana.
  • Para apoyar la hipótesis de la dinamina como la molécula generadora de fuerza en la fisión de la membrana.

Principales métodos:

  • Purificación de la dinamina recombinante.
  • La unión de la dinamina a las bicapas lipídicas.
  • Observación de las interacciones dinamina-lípido utilizando microscopía electrónica (implicado).
  • Adición de GTP para inducir cambios conformacionales y formación de vesículas.

Principales resultados:

  • La dinamina recombinante purificada se autoensambla en las bicapas lipídicas en tubos helicoidales.
  • La adición de GTP causa constricción y vesiculación de estas estructuras dinamina-lípidos.
  • La dinamina por sí sola demuestra la capacidad de formar cuellos constreñidos.

Conclusiones:

  • La dinamina funciona como una enzima mecanoquímica.
  • La dinamina es suficiente para generar las fuerzas requeridas para la fisión de la membrana.
  • Estos hallazgos apoyan el papel único de la dinamina en la formación de vesículas y la escisión de la membrana.