Video Experimental Relacionado

Updated: Aug 7, 2026

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

Published on: December 17, 2012

Una señal di-ácida requerida para la exportación selectiva desde el retículo endoplasmático

N Nishimura¹, W E Balch

¹Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Science (New York, N.Y.)

|July 25, 1997

Resumen

Los investigadores identificaron una señal di-ácida (Asp-X-Glu) esencial para la exportación de proteínas desde el retículo endoplasmático (ER) a través de las vesículas. Este hallazgo sugiere que un mecanismo selectivo gobierna la exportación de ER para proteínas de membrana.

Área de la Ciencia:

Biología celular Biología celular.
Biología Molecular Biología Molecular
Tráfico de proteínas El tráfico de proteínas.

Sus antecedentes:

El transporte intracelular de proteínas de membrana se basa en secuencias citoplasmáticas específicas para el empaque de las vesículas.
La identificación de la señal para la exportación del retículo endoplasmático (ER) ha sido un desafío.

Objetivo del estudio:

Para identificar la secuencia específica que media la exportación desde el retículo endoplasmático (ER).
Investigar el mecanismo de la exportación selectiva desde el ER.

Principales métodos:

Análisis de los dominios citoplasmáticos de las proteínas de la membrana.
Experimentos en células renales de hámster bebé para observar el reclutamiento de proteínas a las vesículas.

Principales resultados:

Se identificó una señal di-ácida (Asp-X-Glu) en la cola citoplasmática de la glicoproteína del virus de la estomatitis vesicular (VSV-G) y otra carga.
Esta señal di-ácida era necesaria para el reclutamiento eficiente de las vesículas mediadoras de la exportación de ER.

Conclusiones:

La señal diácida actúa como un mediador clave para la exportación de ER.
La existencia de esta señal apoya un mecanismo selectivo para la exportación de proteínas desde la ER.

Más Videos Relacionados

Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Functional Characterization of Na⁺/H⁺ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Published on: March 30, 2015

Utilizing pHluorin-tagged Receptors to Monitor Subcellular Localization and Trafficking

Utilizing pHluorin-tagged Receptors to Monitor Subcellular Localization and Trafficking

Published on: March 16, 2017

Videos de Conceptos Relacionados

Nuclear Export

Nuclear Export

The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...

ER Retrieval Pathway

ER Retrieval Pathway

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.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...

Directing Proteins to the Rough Endoplasmic Reticulum

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...

Insertion of Single-pass Transmembrane Proteins in the RER

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...

GPI Anchoring of Proteins in the ER Membrane

GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...

Export of Misfolded Proteins out of the ER

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...