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

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.1K
Exon Recombination02:32

Exon Recombination

3.1K
The evolution of new genes is critical for speciation. Exon recombination, also known as exon shuffling or domain shuffling, is an important means of new gene formation. It is observed across vertebrates, invertebrates, and in some plants such as potatoes and sunflowers. During exon recombination, exons from the same or different genes recombine and produce new exon-intron combinations, which might evolve into new genes. 
Exon shuffling follows “splice frame rules.” Each exon...
3.1K
Complementation Tests00:49

Complementation Tests

4.9K
A complementation test is a simple cross to identify whether the two mutations are located on the same gene or different genes. It was first performed by Edward Lewis in the 1940s while working on fruit flies. He developed the test to identify the location and arrangement of different mutations on chromosomes.
Organisms heterozygous for different mutations are crossed pairwise in all combinations. If present on different genes, the mutations can complement each other by providing the missing...
4.9K
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

2.8K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
2.8K

You might also read

Related Articles

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

Sort by
Same author

Screening and identification of protein-protein interaction using proximity labeling.

Methods in cell biology·2026
Same author

TBBPA-induced insulin reduction in two generations of marine medaka (Oryzias melastigma) with calcium signaling as a key event.

Environmental pollution (Barking, Essex : 1987)·2026
Same author

Anomeric-Effect-Guided Saturated Weakly Solvating Electrolytes for Ultrastable High-Voltage Sodium Metal Batteries.

Angewandte Chemie (International ed. in English)·2026
Same author

Targeting keratin 6 A overcomes gemcitabine resistance by restoring equilibrative nucleoside transporter 1 and TAM-mediated metabolic compensation in pancreatic cancer.

Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy·2026
Same author

Diabetes and Vitiligo.

Diabetes care·2026
Same author

Vis-NIR spectroscopy and deep learning for non-invasive in vivo detection of acute liver injury.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy·2026

Related Experiment Video

Updated: May 5, 2026

Mapping and Application of Enhancer-trap Flippase Expression in Larval and Adult Drosophila CNS
09:45

Mapping and Application of Enhancer-trap Flippase Expression in Larval and Adult Drosophila CNS

Published on: June 3, 2011

16.2K

Functional complementation between FADD and RIP1 in embryos and lymphocytes.

Haibing Zhang1, Xiaohui Zhou, Thomas McQuade

  • 1Department of Microbiology and Immunology, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.

Nature
|March 4, 2011
PubMed
Summary
This summary is machine-generated.

FAS-associated death domain (FADD) protein is crucial for embryogenesis and lymphocyte function. Its interaction with RIP1 kinase unexpectedly regulates both programmed cell death (apoptosis) and necrosis, impacting development and immune responses.

More Related Videos

Dissecting Cell-Autonomous Function of Fragile X Mental Retardation Protein in an Auditory Circuit by In Ovo Electroporation
11:10

Dissecting Cell-Autonomous Function of Fragile X Mental Retardation Protein in an Auditory Circuit by In Ovo Electroporation

Published on: July 6, 2022

1.8K
A GFP Complementation-based Dual-expression System for Assessing Cell-Cell Contact Mediated by Cytonemes in Live Drosophila Wing Imaginal Discs
07:26

A GFP Complementation-based Dual-expression System for Assessing Cell-Cell Contact Mediated by Cytonemes in Live Drosophila Wing Imaginal Discs

Published on: August 22, 2025

720

Related Experiment Videos

Last Updated: May 5, 2026

Mapping and Application of Enhancer-trap Flippase Expression in Larval and Adult Drosophila CNS
09:45

Mapping and Application of Enhancer-trap Flippase Expression in Larval and Adult Drosophila CNS

Published on: June 3, 2011

16.2K
Dissecting Cell-Autonomous Function of Fragile X Mental Retardation Protein in an Auditory Circuit by In Ovo Electroporation
11:10

Dissecting Cell-Autonomous Function of Fragile X Mental Retardation Protein in an Auditory Circuit by In Ovo Electroporation

Published on: July 6, 2022

1.8K
A GFP Complementation-based Dual-expression System for Assessing Cell-Cell Contact Mediated by Cytonemes in Live Drosophila Wing Imaginal Discs
07:26

A GFP Complementation-based Dual-expression System for Assessing Cell-Cell Contact Mediated by Cytonemes in Live Drosophila Wing Imaginal Discs

Published on: August 22, 2025

720

Area of Science:

  • Cell Biology
  • Immunology
  • Developmental Biology

Background:

  • FAS-associated death domain (FADD) protein is a key adaptor in apoptosis signaling via death receptors.
  • While essential for immune homeostasis, FADD's role in embryogenesis and lymphocyte proliferation has been unclear.
  • FADD interacts with RIP1 kinase, which regulates necrosis and NF-κB activation.

Purpose of the Study:

  • To elucidate the in vivo functional interaction between FADD and RIP1.
  • To investigate the roles of FADD and RIP1 in embryogenesis and lymphocyte proliferation.
  • To understand the cell-type-specific interplay between FADD and RIP1.

Main Methods:

  • Generation of Fadd(-/-)Rip1(-/-) double-knockout mice.
  • Analysis of embryonic development and lymphocyte proliferation in knockout models.
  • Assessment of cell death pathways (apoptosis and necrosis) and NF-κB activity.

Main Results:

  • Fadd(-/-) embryos exhibit high RIP1 levels and massive necrosis.
  • RIP1 deficiency rescued embryonic lethality in Fadd(-/-) mice.
  • FADD deletion partially corrected developmental defects in Rip1(-/-) lymphocytes, restoring T cell proliferation but not B cell proliferation.
  • Double-knockout T cells showed resistance to death receptor-induced apoptosis and reduced NF-κB activity.

Conclusions:

  • FADD and RIP1 have a critical, cell-type-specific interplay regulating apoptosis and necrosis.
  • This interaction is essential for embryonic development and lymphocyte function.
  • The findings reveal a novel mechanism controlling cell death and immune responses.