Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

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

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
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

Related Experiment Video

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

A phosphorylation-dependent ubiquitination switch orchestrates nuclear immune reprogramming upon chitin perception.

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
Summary

Rice 14-3-3 proteins OsGF14f and OsGF14c boost resistance to rice blast fungus. Chitin perception triggers a pathway stabilizing these proteins, enhancing plant immunity against Magnaporthe oryzae.

More Related Videos

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

Related Experiment Videos

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

Area of Science:

  • Plant Biology
  • Molecular Plant Pathology
  • Biochemistry

Background:

  • 14-3-3 proteins are crucial for plant growth and stress responses.
  • Their specific roles and regulatory mechanisms in plant immunity are not well understood.

Purpose of the Study:

  • To investigate the function of rice 14-3-3 proteins in immunity against Magnaporthe oryzae.
  • To elucidate the regulatory mechanisms controlling rice plant immunity.

Main Methods:

  • Investigated the function of OsGF14f and OsGF14c in rice.
  • Analyzed the role of E3 ligase OsPUB20 in protein degradation.
  • Studied the effect of chitin perception and OsRLCK185 phosphorylation.
  • Examined protein localization and interactions using microscopy and biochemical assays.

Main Results:

  • OsGF14f and OsGF14c redundantly enhance rice resistance to Magnaporthe oryzae.
  • OsPUB20 targets OsGF14f/OsGF14c for degradation, negatively regulating immunity.
  • Chitin perception activates OsRLCK185, phosphorylating and stabilizing OsPUB20, thereby enhancing resistance.
  • OsGF14f moves to the nucleus, degrading the negative regulator OsWRKY42.

Conclusions:

  • A novel phosphorylation-dependent ubiquitination switch regulates rice immunity.
  • This mechanism links cell surface chitin perception to nuclear defense responses.
  • Findings provide insights into plant immune signaling pathways and potential targets for crop improvement.