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

Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

4.3K
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...
4.3K
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

2.2K
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...
2.2K
The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

6.2K
Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
6.2K
ER Retrieval Pathway01:45

ER Retrieval Pathway

3.8K
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...
3.8K
Autophagic Cell Death01:18

Autophagic Cell Death

3.3K
Christian de Duve discovered “autophagy,” a process in which cellular components are engulfed by membrane-bound organelles called autophagosomes. The autophagosomes then fuse with lysosomes to digest the enclosed contents. Autophagy is generally activated in cells to prevent cell death. However, cell death is triggered when the damage is beyond repair.
Autophagy and Apoptosis
Autophagy can activate apoptosis. In normal conditions, the autophagy activating protein Beclin-1 and...
3.3K
The Unfolded Protein Response01:37

The Unfolded Protein Response

5.6K
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...
5.6K

You might also read

Related Articles

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

Sort by
Same author

LRR-RLK subfamily II of coreceptors: emerging, non-canonical and canonical roles in plant antiviral immunity and development.

Frontiers in plant science·2025
Same author

The immune NIK1/RPL10/LIMYB signaling module regulates photosynthesis and translation under biotic and abiotic stresses.

Nature communications·2025
Same author

Decoding the senses: A new player in plant-virus dynamics unveiled.

Molecular plant·2025
Same author

A Nutritional Strategy Based on Multiple Components for Glycemic Control in Type 2 Diabetes: A Multicenter Randomized Controlled Clinical Trial.

Nutrients·2024
Same author

The complete genome sequence of "<i>Candidatus</i> Liberibacter asiaticus" strain 9PA and the characterization of field strains in the Brazilian citriculture.

mSphere·2024
Same author

Expansion and diversification of the Glycine max (Gm) ERD15-like subfamily of the PAM2-like superfamily.

Planta·2024

Related Experiment Video

Updated: May 5, 2026

Examining BCL-2 Family Function with Large Unilamellar Vesicles
08:35

Examining BCL-2 Family Function with Large Unilamellar Vesicles

Published on: October 5, 2012

7.4K

The endoplasmic reticulum binding protein BiP displays dual function in modulating cell death events.

Humberto H Carvalho1, Priscila A Silva, Giselle C Mendes

  • 1National Institute of Science and Technology in Plant-Pest Interactions , Universidade Federal de Viçosa, 36570.000, Viçosa, Minas Gerais, Brazil.

Plant Physiology
|December 10, 2013
PubMed
Summary

Binding protein (BiP) modulates programmed cell death (PCD) in plants. BiP delays leaf senescence by inhibiting cell death signaling but accelerates hypersensitive PCD during pathogen attack, acting as a dual regulator.

More Related Videos

Identifying Protein-protein Interaction Sites Using Peptide Arrays
07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

17.7K
Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons
10:50

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons

Published on: April 24, 2021

1.1K

Related Experiment Videos

Last Updated: May 5, 2026

Examining BCL-2 Family Function with Large Unilamellar Vesicles
08:35

Examining BCL-2 Family Function with Large Unilamellar Vesicles

Published on: October 5, 2012

7.4K
Identifying Protein-protein Interaction Sites Using Peptide Arrays
07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

17.7K
Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons
10:50

Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons

Published on: April 24, 2021

1.1K

Area of Science:

  • Plant molecular biology
  • Cell death regulation
  • Plant immunity

Background:

  • Binding protein (BiP) is known to be involved in innate immunity and stress-induced cell death.
  • The role of BiP in developmental and hypersensitive programmed cell death (PCD) in plants remains to be fully elucidated.
  • Endoplasmic reticulum (ER) stress and unfolded protein response (UPR) are implicated in cellular homeostasis and stress responses.

Purpose of the Study:

  • To investigate the role of BiP in controlling developmental and hypersensitive programmed cell death (PCD) in plants.
  • To determine how manipulated BiP levels affect plant responses to stress and pathogen interactions.
  • To elucidate the molecular mechanisms underlying BiP's dual role in PCD regulation.

Main Methods:

  • Utilized transgenic plants with altered BiP expression levels (overexpression and potentially knockdown).
  • Analyzed transcriptomic changes in BiP-manipulated plants under normal and stress conditions.
  • Assessed hallmarks of PCD, including leaf senescence and hypersensitive response (HR) to pathogen challenge (Pseudomonas syringae pv tomato) in soybean and tobacco.

Main Results:

  • BiP overexpression led to down-regulation of developmental PCD genes and up-regulation of hypersensitive PCD genes.
  • BiP-overexpressing plants showed delayed leaf senescence and accelerated HR, indicating differential regulation of PCD.
  • BiP's regulation of senescence involved attenuation of N-rich protein (NRP)-mediated cell death signaling and UPR, while during HR, it positively regulated NRP signaling independently of UPR.

Conclusions:

  • BiP acts as a dual modulator of PCD in plants, negatively regulating developmental cell death (senescence) and positively regulating hypersensitive PCD.
  • BiP's function in senescence is linked to attenuating UPR and NRP signaling, whereas its role in hypersensitive PCD is activated by salicylic acid (SA) signaling.
  • The SA-mediated induction of NRP cell death signaling during hypersensitive PCD operates via a pathway distinct from UPR, with BiP positively regulating this process.