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

3.9K
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,...
3.9K
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.1K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.1K
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.5K
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...
12.5K
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

6.6K
Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
6.6K

You might also read

Related Articles

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

Sort by
Same author

Extracellular vesicles from wild-type Epstein-Barr virus-transformed B-cells export host DNA and EBV EBER1.

bioRxiv : the preprint server for biology·2026
Same author

Advances in antioxidant activities of edible mushroom polysaccharides: status, influencing factors, mechanisms, and applications.

Frontiers in nutrition·2026
Same author

A whole genomic CRISPR-Cas9 screen identifies the amino acid transporter SLC43A1 (LAT3) as a major determinant of oxaliplatin sensitivity in colorectal cancer cells.

Molecular cancer therapeutics·2026
Same author

Global Proteomics Investigation of SAMT-247 Targets: An Antiviral Thioester that Acetylates Zinc Finger Proteins.

bioRxiv : the preprint server for biology·2026
Same author

Complement Factor H as a Novel Predictive Biomarker for Deep Vein Thrombosis Recurrence: A Prospective Cohort Study.

Journal of thrombosis and thrombolysis·2026
Same author

Knowledge, Attitude, Practice, and Awareness Regarding Disease Management Among Patients with Chronic Lower Limb Ischemia: A Cross-Sectional Study.

Patient preference and adherence·2026
Same journal

Identification of Age-Associated Circulating Proteins and Lipids in 3800 Comorbidity-Enriched Older Adults from Japan-Based Cohorts Using Olink Assays and MRM Mass Spectrometry.

Journal of proteome research·2026
Same journal

Molecular Solution to the Paradox of Ancient Brain Preservation.

Journal of proteome research·2026
Same journal

From Method-Defined Signals to Reference Measurement Procedures: Two Decades of Mass Spectrometry-Based ProGRP Quantification.

Journal of proteome research·2026
Same journal

Proteomic Profiling of Extracellular Vesicle-Enriched Plasma Using Mag-Net for Biomarker Discovery in Pancreatic Ductal Adenocarcinoma.

Journal of proteome research·2026
Same journal

Computationally Efficient Bayesian Estimation of Graphical Networks for Omics Data.

Journal of proteome research·2026
Same journal

Hierarchy of MS-Based Evidence.

Journal of proteome research·2026
See all related articles

Related Experiment Video

Updated: Jun 14, 2025

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
06:01

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

7.2K

Mapping Extracellular Protein-Protein Interactions Using Extracellular Proximity Labeling (ePL).

David Peeney1, Sadeechya Gurung1, Joshua A Rich1

  • 1Laboratory of Pathology, Center for Cancer Research, National Cancer Institute, Bethesda, Maryland 20892, United States.

Journal of Proteome Research
|September 6, 2024
PubMed
Summary
This summary is machine-generated.

Researchers developed extracellular proximity labeling (ePL) to study protein-protein interactions (PPIs) outside cells. This method revealed the TIMP2 interactome, offering new insights into extracellular matrix regulation and potential therapeutic targets.

Keywords:
interactomicsmatrisomeproximity labeling

More Related Videos

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
11:40

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

2.4K
In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
00:08

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

7.0K

Related Experiment Videos

Last Updated: Jun 14, 2025

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
06:01

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

7.2K
Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics
11:40

Characterization of Neuronal Lysosome Interactome with Proximity Labeling Proteomics

Published on: June 23, 2022

2.4K
In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
00:08

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

7.0K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Proximity labeling (PL) is crucial for studying protein-protein interactions (PPIs) in living cells.
  • Current PL methods primarily focus on intracellular targets, limiting extracellular interaction studies.
  • The extracellular matrix (ECM) and its regulators, like TIMP2, are vital in disease progression and therapeutic development.

Purpose of the Study:

  • To adapt proximity labeling for investigating extracellular PPIs, termed extracellular PL (ePL).
  • To characterize the TIMP2 proximal interactome using the novel ePL technique.
  • To demonstrate the versatility of ePL in various biological contexts.

Main Methods:

  • Development and application of extracellular proximity labeling (ePL) using BioID2/TurboID fusion proteins.
  • Investigated the interactome of the matrisome protein TIMP2.
  • Analyzed PPIs under diverse conditions: different stimuli, cell types, culture formats (2D vs. 3D), and reaction kinetics.

Main Results:

  • Successfully mapped the TIMP2 proximal interactome (MassIVE MSV000095637).
  • Demonstrated dynamic changes in the TIMP2 interactome influenced by experimental conditions.
  • Highlighted the advantages of ePL over traditional PPI methods in capturing context-specific interactions.

Conclusions:

  • Extracellular PL (ePL) is a powerful tool for exploring extracellular PPIs.
  • The TIMP2 interactome is dynamic and context-dependent.
  • ePL screening in disease models can identify novel therapeutic targets for ECM-related diseases.