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

Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:

You might also read

Related Articles

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

Sort by
Same author

Direct radiation exposure of the eye lenses in cranial computed tomography and exposure reduction through radiographer training.

Radiography (London, England : 1995)·2022
Same author

Genetic testing approaches for hereditary breast cancer: Perspectives from a private diagnostic laboratory.

South African medical journal = Suid-Afrikaanse tydskrif vir geneeskunde·2020
Same author

Patient-Clinician Brain Response During Clinical Encounter and Pain Treatment.

Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual International Conference·2020
Same author

Predicting outcomes after acute reperfusion therapy for basilar artery occlusion.

European journal of neurology·2020
Same author

Current Status of Indications, Timing, Management, Complications, and Outcomes of Tracheostomy in Traumatic Brain Injury Patients.

Journal of neurosciences in rural practice·2020
Same author

New recurring BRCA1 variant: An additional South African founder mutation?

South African medical journal = Suid-Afrikaanse tydskrif vir geneeskunde·2019

Related Experiment Video

Updated: Jun 29, 2026

Subcloning Plus Insertion (SPI) - A Novel Recombineering Method for the Rapid Construction of Gene Targeting Vectors
09:02

Subcloning Plus Insertion (SPI) - A Novel Recombineering Method for the Rapid Construction of Gene Targeting Vectors

Published on: January 8, 2015

The p400 complex is an essential E1A transformation target.

M Fuchs1, J Gerber, R Drapkin

  • 1Dana-Farber Cancer Institute, Boston, MA, USA.

Cell
|August 18, 2001
PubMed
Summary
This summary is machine-generated.

Researchers identified a new E1A binding protein complex, crucial for E1A-mediated transformation. The core component, p400, and its associated proteins are vital for this process, highlighting their role in cell transformation.

More Related Videos

An Ecdysone Receptor-based Singular Gene Switch for Deliberate Expression of Transgene with Robustness, Reversibility, and Negligible Leakiness
06:21

An Ecdysone Receptor-based Singular Gene Switch for Deliberate Expression of Transgene with Robustness, Reversibility, and Negligible Leakiness

Published on: May 7, 2018

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

Published on: May 1, 2020

Related Experiment Videos

Last Updated: Jun 29, 2026

Subcloning Plus Insertion (SPI) - A Novel Recombineering Method for the Rapid Construction of Gene Targeting Vectors
09:02

Subcloning Plus Insertion (SPI) - A Novel Recombineering Method for the Rapid Construction of Gene Targeting Vectors

Published on: January 8, 2015

An Ecdysone Receptor-based Singular Gene Switch for Deliberate Expression of Transgene with Robustness, Reversibility, and Negligible Leakiness
06:21

An Ecdysone Receptor-based Singular Gene Switch for Deliberate Expression of Transgene with Robustness, Reversibility, and Negligible Leakiness

Published on: May 7, 2018

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

Published on: May 1, 2020

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Oncology

Background:

  • The E1A protein is a key viral oncoprotein known to induce cellular transformation.
  • Understanding the molecular mechanisms underlying E1A-mediated transformation is crucial for cancer research.

Purpose of the Study:

  • To identify and characterize novel protein complexes interacting with E1A.
  • To elucidate the role of these complexes in E1A-mediated cellular transformation.

Main Methods:

  • Co-immunoprecipitation assays to identify E1A binding partners.
  • Biochemical characterization of the identified protein complex.
  • Functional assays using E1A mutants and protein fragments to assess transformation activity.

Main Results:

  • Identification of a novel E1A binding protein complex containing p400 as the core component.
  • Demonstration that the E1A-p400 complex is essential for E1A-mediated transformation.
  • Evidence that E1A and c-myc can modulate the subunit composition of p400 complexes.

Conclusions:

  • The E1A-p400 complex plays a critical role in the E1A transforming process.
  • Alterations in p400 complex composition by E1A and c-myc suggest a role in transformation suppression.