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

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

9.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
9.8K
Regulated Protein Degradation02:58

Regulated Protein Degradation

9.0K
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...
9.0K
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

3.1K
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...
3.1K
The Unfolded Protein Response01:37

The Unfolded Protein Response

6.5K
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...
6.5K
Phosphorylation01:02

Phosphorylation

54.7K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
54.7K
Receptor Downregulation in MVBs01:15

Receptor Downregulation in MVBs

2.9K
Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
2.9K

También podría leer

Artículos Relacionados

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

Ordenar por
Same author

Dual regulation of RNase P subunit Rpp30 by an acetyltransferase and E3 ligase in rice immunity.

Plant physiology·2026
Same author

A Conserved Magnaporthe oryzae Effector Counteracts the Rice Ubiquitin-Proteasome System by Disrupting the E2 Function to Suppress Immunity.

Plant biotechnology journal·2026
Same author

E3 ubiquitin ligase-mediated degradation of Rab GTPase suppresses an MAPKK and activates immunity in rice.

Journal of integrative plant biology·2026
Same author

Balancing rice blast resistance and growth through suppression of the E3 ubiquitin ligase OsRING80.

Plant physiology·2025
Same author

Phosphorylation and ubiquitination synergistically promote the degradation of OsRbohB to modulate rice immunity.

The Plant cell·2025
Same author

Natural variation in SBRR1 shows high potential for sheath blight resistance breeding in rice.

Nature genetics·2025

Video Experimental Relacionado

Updated: Feb 23, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
07:58

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

Published on: January 2, 2026

416

Un interruptor de ubiquitinación dependiente de la fosforilación orquesta la reprogramación inmune nuclear después de

Chongyang Zhang1,2,3, Pavinee Suttiviriya2, Ruyi Wang1

  • 1State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China.

Nature communications
|February 21, 2026
PubMed
Resumen

Las proteínas del arroz 14-3-3 OsGF14f y OsGF14c aumentan la resistencia al hongo del chorro de arroz. La percepción de la quitina desencadena una vía que estabiliza estas proteínas, mejorando la inmunidad de la planta contra Magnaporthe oryzae.

Más Videos Relacionados

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

11.5K
Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

24.7K

Videos de Experimentos Relacionados

Last Updated: Feb 23, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
07:58

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination

Published on: January 2, 2026

416
In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

11.5K
Identification of Post-translational Modifications of Plant Protein Complexes
10:07

Identification of Post-translational Modifications of Plant Protein Complexes

Published on: February 22, 2014

24.7K

Área de la Ciencia:

  • Biología Vegetal Biología Vegetal
  • Patología Molecular de las Plantas Patología Molecular.
  • La bioquímica es la bioquímica.

Sus antecedentes:

  • Las proteínas 14-3-3 son cruciales para el crecimiento de las plantas y las respuestas al estrés.
  • Sus funciones específicas y mecanismos reguladores en la inmunidad vegetal no se comprenden bien.

Objetivo del estudio:

  • Investigar la función de las proteínas 14-3-3 del arroz en la inmunidad contra Magnaporthe oryzae.
  • Para aclarar los mecanismos regulatorios que controlan la inmunidad de la planta del arroz.

Principales métodos:

  • Investigó la función de OsGF14f y OsGF14c en el arroz.
  • Analizó el papel de la E3 ligasa OsPUB20 en la degradación de las proteínas.
  • Estudió el efecto de la percepción de la quitina y la fosforilación de OsRLCK185.
  • Examinó la localización de proteínas e interacciones usando microscopía y ensayos bioquímicos.

Principales resultados:

  • OsGF14f y OsGF14c aumentan redundantemente la resistencia del arroz a las Magnaporthe oryzae.
  • OsPUB20 se dirige a OsGF14f/OsGF14c para su degradación, regulando negativamente la inmunidad.
  • La percepción de la quitina activa OsRLCK185, fosforila y estabiliza OsPUB20, mejorando así la resistencia.
  • OsGF14f se mueve hacia el núcleo, degradando el regulador negativo OsWRKY42.

Conclusiones:

  • Un nuevo interruptor de ubiquitinación dependiente de la fosforilación regula la inmunidad del arroz.
  • Este mecanismo vincula la percepción de la quitina en la superficie celular con las respuestas de defensa nuclear.
  • Los hallazgos proporcionan información sobre las vías de señalización inmune de las plantas y los posibles objetivos para la mejora de los cultivos.