Jove
Visualize
Contáctanos
JoVE
x logofacebook logolinkedin logoyoutube logo
ACERCA DE JoVE
Visión GeneralLiderazgoBlogCentro de Ayuda JoVE
AUTORES
Proceso de PublicaciónConsejo EditorialAlcance y PolíticasRevisión por ParesPreguntas FrecuentesEnviar
BIBLIOTECARIOS
TestimoniosSuscripcionesAccesoRecursosConsejo Asesor de BibliotecasPreguntas Frecuentes
INVESTIGACIÓN
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchivo
EDUCACIÓN
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualCentro de Recursos para ProfesoresSitio de Profesores
Términos y Condiciones de Uso
Política de Privacidad
Políticas

Videos de Conceptos Relacionados

The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...

También podría leer

Artículos Relacionados

Artículos vinculados a este trabajo por autores compartidos, revista y gráfico de citas.

Ordenar por
Same author

<i>Siphoviridae</i> phage tails co-enrich with ex vivo amyloids.

bioRxiv : the preprint server for biology·2026
Same author

Small molecule stabilization of diverse amyloidogenic immunoglobulin light chains revealed by hydrogen-deuterium exchange mass spectrometry.

Journal of molecular biology·2026
Same author

Helical reconstruction of amyloids in cryoSPARC.

Acta crystallographica. Section F, Structural biology communications·2026
Same author

Molecular and Structural Characterization Reveals Divergent Extracellular Vesicle Profiles Between Wild Type and Alzheimer's Disease Cerebrocortical Organoids.

bioRxiv : the preprint server for biology·2026
Same author

Impaired lipoprotein secretion by APOE4 leads to lysosomal and mitochondrial dysfunction in human microglia.

bioRxiv : the preprint server for biology·2026
Same author

Three-Dimensional Visualization and Proteomic Analysis of Human Cardiac Transthyretin Amyloidosis Tissue Reveals Microangiopathy and Capillary Occlusion.

Journal of the American Heart Association·2026
Same journal

Erratum for the Research Article "Detecting supramolecular organic nanoparticles during heat wave".

Science (New York, N.Y.)·2026
Same journal

Local signals, systemic decline.

Science (New York, N.Y.)·2026
Same journal

The mechanics of liver regeneration.

Science (New York, N.Y.)·2026
Same journal

Computing in a memory with physics.

Science (New York, N.Y.)·2026
Same journal

Retraction.

Science (New York, N.Y.)·2026
Same journal

Making time.

Science (New York, N.Y.)·2026
Ver todos los artículos relacionados

Video Experimental Relacionado

Updated: Jul 7, 2026

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
09:18

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Published on: September 7, 2021

Adaptación de la proteostasis para la intervención en enfermedades.

William E Balch1, Richard I Morimoto, Andrew Dillin

  • 1Department of Cell Biology and Institute for Childhood and Neglected Diseases, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Science (New York, N.Y.)
|February 16, 2008
PubMed
Resumen
Este resumen es generado por máquina.

El mantenimiento de la homeostasis proteica (proteostasis) es vital para la salud celular, el desarrollo y la prevención de enfermedades. La red de proteostasis regula la integridad de las proteínas, y su disfunción causa numerosos trastornos.

Más Videos Relacionados

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
12:38

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

Published on: December 18, 2013

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Videos de Experimentos Relacionados

Last Updated: Jul 7, 2026

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans
09:18

Quantifying Tissue-Specific Proteostatic Decline in Caenorhabditis elegans

Published on: September 7, 2021

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism
12:38

Using Caenorhabditis elegans as a Model System to Study Protein Homeostasis in a Multicellular Organism

Published on: December 18, 2013

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Área de la Ciencia:

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

Sus antecedentes:

  • Las células eucariotas se enfrentan constantemente a amenazas a la integridad de las proteínas.
  • La homeostasis proteica (proteostasis) es crucial para el desarrollo saludable, el envejecimiento y la prevención de enfermedades.
  • La proteostasis disfuncional está relacionada con varias enfermedades, incluyendo trastornos metabólicos, oncológicos, neurodegenerativos y cardiovasculares.

Objetivo del estudio:

  • Describir la red de proteostasis y su papel en el mantenimiento de la salud celular y del organismo.
  • Para resaltar el potencial terapéutico de dirigirse a la red de proteostasis para el tratamiento de enfermedades.

Principales métodos:

  • Este estudio proporciona una descripción general de la red de proteostasis.
  • Se discuten los mecanismos involucrados en el mantenimiento de la integridad de las proteínas dentro de las células eucariotas.

Principales resultados:

  • La red de proteostasis comprende actividades en interacción esenciales para la salud del proteoma.
  • Las deficiencias en la proteostasis están implicadas en una amplia gama de enfermedades graves.
  • Dirigirse a los reguladores de la proteostasis ofrece estrategias terapéuticas potenciales.

Conclusiones:

  • La red de proteostasis es fundamental para el bienestar celular y del organismo.
  • Comprender y manipular la proteostasis es prometedor para el tratamiento de enfermedades difíciles.