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

Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

2.9K
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...
2.9K
PI3K/mTOR/AKT Signaling Pathway01:22

PI3K/mTOR/AKT Signaling Pathway

5.1K
The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
5.1K
Negative Regulator Molecules01:23

Negative Regulator Molecules

38.1K
Positive regulators allow a cell to advance through cell cycle checkpoints. Negative regulators have an equally important role as they terminate a cell’s progression through the cell cycle—or pause it—until the cell meets specific criteria.
38.1K
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

4.5K
The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
4.5K
MAPK Signaling Cascades01:07

MAPK Signaling Cascades

7.7K
Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
7.7K
The Unfolded Protein Response01:37

The Unfolded Protein Response

6.1K
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...
6.1K

You might also read

Related Articles

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

Sort by
Same author

Dimerization Promotes PKR Activation by Modulating Energetics of αC Helix Conversion between Active and Inactive Conformations.

The journal of physical chemistry. B·2024
Same author

Human cytomegalovirus protein RL1 degrades the antiviral factor SLFN11 via recruitment of the CRL4 E3 ubiquitin ligase complex.

Proceedings of the National Academy of Sciences of the United States of America·2022
Same author

Contribution of dsRBD2 to PKR Activation.

ACS omega·2021
Same author

Oligomerization of RIG-I and MDA5 2CARD domains.

Protein science : a publication of the Protein Society·2019
Same author

Structural Basis of Protein Kinase R Autophosphorylation.

Biochemistry·2019
Same author

Design of High-Affinity Metal-Controlled Protein Dimers.

Biochemistry·2019

Related Experiment Video

Updated: Dec 26, 2025

Isolation and Quantification of Epstein-Barr Virus from the P3HR1 Cell Line
09:14

Isolation and Quantification of Epstein-Barr Virus from the P3HR1 Cell Line

Published on: September 28, 2022

4.4K

Regulation of Protein Kinase R by Epstein-Barr Virus EBER1 RNA.

Cassie M Zerbe, James L Cole

    Biochemistry
    |March 17, 2020
    PubMed
    Summary

    Epstein-Barr virus EBER1 RNA weakly activates Protein Kinase R (PKR), unlike VAI RNA which acts as a decoy. EBER1 binds PKR less strongly, suggesting it

    Area of Science:

    • Virology
    • Immunology
    • Structural Biology

    Background:

    • Protein kinase R (PKR) is a crucial antiviral protein activated by viral double-stranded RNAs (dsRNAs).
    • Noncoding viral RNAs like Adenovirus-associated RNA 1 (VAI) and Epstein-Barr virus EBER1 can modulate PKR activity.
    • VAI RNA inhibits PKR activation by binding it without inducing activation, acting as a decoy.

    Purpose of the Study:

    • To compare the interactions of PKR with VAI and EBER1.
    • To present a structural model of EBER1.
    • To elucidate the mechanisms by which these RNAs modulate the innate immune response.

    Main Methods:

    • Comparative analysis of RNA-PKR interactions.
    • Structural modeling of EBER1 using chemical structure probing and small-angle X-ray scattering.

    More Related Videos

    Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle
    10:05

    Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

    Published on: March 5, 2019

    6.8K
    Functional Characterization of Endogenously Expressed Human RYR1 Variants
    07:59

    Functional Characterization of Endogenously Expressed Human RYR1 Variants

    Published on: June 9, 2021

    2.9K

    Related Experiment Videos

    Last Updated: Dec 26, 2025

    Isolation and Quantification of Epstein-Barr Virus from the P3HR1 Cell Line
    09:14

    Isolation and Quantification of Epstein-Barr Virus from the P3HR1 Cell Line

    Published on: September 28, 2022

    4.4K
    Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle
    10:05

    Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle

    Published on: March 5, 2019

    6.8K
    Functional Characterization of Endogenously Expressed Human RYR1 Variants
    07:59

    Functional Characterization of Endogenously Expressed Human RYR1 Variants

    Published on: June 9, 2021

    2.9K
  • Biochemical assays to assess PKR activation and binding affinity at physiological ion concentrations.

    • Main Results:

    • Both VAI and EBER1 inhibit dsRNA-mediated PKR activation.
    • EBER1 weakly activates PKR, whereas VAI does not.
    • PKR binds EBER1 more weakly than VAI, and both RNAs can induce PKR dimerization.

    Conclusions:

    • EBER1's structural features, including an extended RNA duplex, mediate PKR binding and activation.
    • EBER1 is less effective as an RNA decoy compared to VAI due to weaker binding and weak activation of PKR.
    • These findings provide insights into viral immune evasion strategies involving noncoding RNAs and PKR modulation.