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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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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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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
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TRAPPI ata las vesículas COPII mediante la unión de la subunidad de capa Sec2323

Huaqing Cai1, Sidney Yu, Shekar Menon

  • 1Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06519, USA.

Nature
|February 9, 2007
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Resumen

El complejo de conexión de TRAPP I se une a la subunidad de capa COPII Sec23, mediada por Bet3. Esta interacción apunta TRAPP I a las vesículas, facilitando su fusión con las membranas diana.

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Área de la Ciencia:

  • Biología celular Biología celular.
  • Biología Molecular Biología Molecular
  • El tráfico de membranas.

Sus antecedentes:

  • El brote de las vesículas desde el retículo endoplasmático (ER) depende del complejo de capa COPII.
  • El montaje de la capa implica los adaptadores Sar1-GTP, Sec23/24 y el complejo de polimerización Sec13/31.
  • La unión de las vesículas a las membranas objetivo está mediada por factores de unión específicos.

Objetivo del estudio:

  • Para investigar la interacción entre la maquinaria de fijación de vesículas y la capa COPII.
  • Para identificar los componentes moleculares involucrados en la orientación de las ataduras a las vesículas COPII.
  • Para entender cómo los complejos de atadura son reclutados para transportar las vesículas.

Principales métodos:

  • Análisis bioquímicos en extractos de levadura y células de mamíferos.
  • Estudios de unión in vitro.
  • Análisis de las interacciones proteína-proteína entre la capa y los factores de atadura.

Principales resultados:

  • El complejo de enlace TRAPP I se une directamente a la subunidad de capa COPII Sec23.3.
  • Esta interacción es dependiente de la subunidad Bet3 de TRAPP I.
  • Los estudios in vitro confirman que la interacción de Sec23-Bet3 se dirige a las vesículas TRAPP I a COPII para el enlace.

Conclusiones:

  • TRAPP I es reclutado para las vesículas COPII a través de la interacción con Sec23, mediada por Bet3.
  • Este mecanismo asegura el enlace adecuado de las vesículas a sus membranas diana.
  • El complejo de capa y su carga asociada juegan un papel en la determinación del destino de las vesículas.