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 Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
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...
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...

You might also read

Related Articles

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

Sort by
Same author

Author Correction: Matrix viscoelasticity promotes liver cancer progression in the pre-cirrhotic liver.

Nature·2025
Same author

Circadian regulator REV-ERBα is a master regulator of tumor lineage plasticity and an effective therapeutic target.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

A novel isoform of tensin-1 promotes actin filament assembly for efficient erythroblast enucleation.

Blood advances·2025
Same author

circFUT8 promotes proplatelet formation by interacting with IGF2BP2 and stabilizing TNS1 mRNA in megakaryocytes.

Blood·2025
Same author

A novel isoform of Tensin1 promotes actin filament assembly for efficient erythroblast enucleation.

bioRxiv : the preprint server for biology·2025
Same author

Tandem LIM domain-containing proteins, LIMK1 and LMO1, directly bind to force-bearing keratin intermediate filaments.

Cell reports·2024

Related Experiment Video

Updated: Jul 16, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

Reverse interactomics: from peptides to proteins and to functions.

Su Hao Lo1

  • 1Lawrence Ellison Center for Tissue Regeneration and Repair, Department of Orthopaedic Surgery, Cancer Center, University of California-Davis, Sacramento, California 95817, USA. shlo@ucdavis.edu

ACS Chemical Biology
|February 23, 2007
PubMed
Summary

This study introduces "reverse interactomics" to find binding partners for the tensin Src homology 2 (SH2) domain. This method helps understand protein function and signaling pathways in cell biology.

More Related Videos

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

mRNA Interactome Capture from Plant Protoplasts
12:29

mRNA Interactome Capture from Plant Protoplasts

Published on: July 28, 2017

Related Experiment Videos

Last Updated: Jul 16, 2026

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
09:10

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

Mapping Dysfunctional Protein-Protein Interactions in Disease
09:39

Mapping Dysfunctional Protein-Protein Interactions in Disease

Published on: October 24, 2025

mRNA Interactome Capture from Plant Protoplasts
12:29

mRNA Interactome Capture from Plant Protoplasts

Published on: July 28, 2017

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Proteomics

Background:

  • Identifying protein interaction partners is crucial for elucidating molecular functions and signaling pathways.
  • The Src homology 2 (SH2) domain specifically binds to phosphotyrosine residues, playing a key role in signal transduction.
  • Tensin is a protein implicated in various cellular processes, and understanding its interactome is important.

Purpose of the Study:

  • To identify novel binding partners of the tensin SH2 domain.
  • To demonstrate the utility of "reverse interactomics" for discovering protein-protein interactions.
  • To provide insights into the functional context of tensin within cellular signaling networks.

Main Methods:

  • Application of "reverse interactomics" strategy.
  • Utilizing the SH2 domain of tensin as the bait.
  • Analysis of identified binding partners to infer functional associations.

Main Results:

  • Successful identification of specific binding partners for the tensin SH2 domain.
  • Demonstration that "reverse interactomics" is an effective approach for partner discovery.
  • Generated a list of potential interactors that can be further investigated.

Conclusions:

  • "Reverse interactomics" is a powerful tool for identifying SH2 domain binding partners.
  • The identified partners offer new avenues for exploring tensin's role in cellular signaling.
  • This approach facilitates a deeper understanding of molecular mechanisms in cell biology.