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

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 to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

You might also read

Related Articles

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

Sort by
Same author

Towards the construction of a virtual yeast.

Nature·2026
Same author

SCM-1/SCAMP Maintains Microdomain Boundaries and Cargo Sorting within the Endosomal System.

bioRxiv : the preprint server for biology·2026
Same author

The novel antifungal agent NPD2560 perturbs the Rho1-centered signaling network to induce a cell wall integrity response.

Microbiology spectrum·2026
Same author

Orobas: A computational approach for scoring and analysis of quantitative chemical-genetic interactions from CRISPR-Cas9 screens.

STAR protocols·2026
Same author

Population-scale chemical response revealed by a barcoded yeast collection.

Nature communications·2026
Same author

Global genetic interaction network of a human cell maps conserved principles and informs functional interpretation of gene co-essentiality profiles.

Cell·2026
Same journal

Paradoxical non-catalytic kinase functions are driven by inhibitor-induced displacement of autoinhibitory domains.

Molecular systems biology·2026
Same journal

E. coli prepares for starvation by dramatically remodeling its proteome in the first hours after loss of nutrients.

Molecular systems biology·2026
Same journal

Common xenobiotics modulate gut microbial responses to low‑calorie sweeteners in vitro.

Molecular systems biology·2026
Same journal

ParTIpy: a scalable framework for archetypal analysis and Pareto task inference.

Molecular systems biology·2026
Same journal

Quantitative interactome mapping of skeletal muscle insulin resistance.

Molecular systems biology·2026
Same journal

Interpretable multi-omics integration across mixed-order tensors with MANTRA.

Molecular systems biology·2026
See all related articles

Related Experiment Video

Updated: May 12, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

SH3 interactome conserves general function over specific form.

Xiaofeng Xin1, David Gfeller, Jackie Cheng

  • 1The Donnelly Centre, University of Toronto, Toronto, Ontario, Canada.

Molecular Systems Biology
|April 4, 2013
PubMed
Summary
This summary is machine-generated.

Src homology 3 (SH3) domains are key for protein interactions. Comparing worm and yeast SH3 networks reveals conserved functions but distinct interaction rewiring, suggesting general network function is preserved during evolution.

More Related Videos

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

Related Experiment Videos

Last Updated: May 12, 2026

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
05:08

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Systems Biology

Background:

  • Src homology 3 (SH3) domains mediate protein-protein interactions crucial for cellular processes.
  • Understanding the evolution and conservation of protein interaction networks provides insights into biological regulation.

Purpose of the Study:

  • To survey SH3 domain binding specificity in Caenorhabditis elegans.
  • To map the worm SH3 interactome and compare it with Saccharomyces cerevisiae.
  • To investigate the evolutionary conservation and rewiring of SH3-mediated interaction networks.

Main Methods:

  • Peptide phage display was used to determine SH3 binding specificity in C. elegans.
  • Yeast two-hybrid assays were employed to map the worm SH3 interactome.
  • Comparative analysis of worm and yeast SH3 networks was performed.

Main Results:

  • The SH3 binding specificity repertoire in C. elegans structurally mirrors that of S. cerevisiae.
  • The worm SH3 interactome is significantly enriched for proteins involved in endocytosis, similar to yeast.
  • Orthologous SH3 domain-mediated interactions show substantial rewiring between the two species.

Conclusions:

  • The general function of SH3 domain networks is conserved across species.
  • Specific SH3-mediated interactions are rewired during evolution, indicating network plasticity.
  • A model of network evolution where general function is conserved over specific interactions is proposed.