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Intralumenal Vesicles and Multivesicular Bodies

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...
Rab Proteins01:14

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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.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
ER Retrieval Pathway01:45

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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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...
Post-translational Translocation of Proteins to the RER01:27

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Targeting proteins to the ER
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Video Experimental Relacionado

Updated: Jul 6, 2026

Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
10:53

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Published on: November 8, 2013

El reconocimiento ESCRT-III por las ATPasas VPS4

Melissa D Stuchell-Brereton1, Jack J Skalicky, Collin Kieffer

  • 1Department of Biochemistry, Room 4100, 15 N. Medical Drive East, University of Utah, Salt Lake City, Utah 84112-5650, USA.

Nature
|October 12, 2007
PubMed
Resumen

Los investigadores descubrieron cómo las ATPasas VPS4 reconocen las proteínas ESCRT-III (CHMP) para impulsar la fisión de la membrana para el brote del VIH, la clasificación endosómica y la división celular. Este mecanismo es crucial para la liberación de virus, vesículas y células hijas.

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Published on: December 21, 2019

Área de la Ciencia:

  • Biología celular Biología celular.
  • Biología Molecular Biología Molecular
  • Virología Virología.

Sus antecedentes:

  • El complejo de clasificación endosómica requerido para la vía de transporte (ESCRT) es vital para la fisión de la membrana en procesos como el brote del VIH y la citocinesis.
  • Las ATPasas VPS4 son clave para esta vía, desmontando los complejos ESCRT-III en las membranas.

Objetivo del estudio:

  • Para dilucidar el mecanismo molecular por el cual las ATPasas VPS4 reconocen e interactúan con las proteínas ESCRT-III.
  • Para entender cómo esta interacción facilita los eventos de fisión de la membrana.

Principales métodos:

  • Análisis estructural de los complejos VPS4A MIT-CHMP1A y VPS4B MIT-CHMP2B.
  • Mutagénesis dirigida al sitio para investigar las interacciones de unión.
  • Pruebas funcionales que evalúan el reclutamiento de VPS4, la clasificación endosómica y el brote del VIH.

Principales resultados:

  • Los dominios de interacción y transporte de microtúbulos (MIT) de VPS4A y VPS4B se unen a motivos conservados en las proteínas CHMP1-3.
  • Los estudios estructurales revelaron un modo de unión único del motivo CHMP dentro del dominio VPS4 MIT.
  • Las mutaciones que interrumpieron esta interacción afectaron la función VPS4 en múltiples procesos celulares.

Conclusiones:

  • Las ATPasas VPS4 reconocen los sustratos CHMP a través de interacciones específicas dentro del dominio MIT.
  • Este mecanismo de reconocimiento es esencial para mediar la fisión de la membrana en la liberación viral, el tráfico endosómico y la división celular.