Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...

Protein Networks

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,...

You might also read

Related Articles

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

Sort by

Same author

PBMC circRNA Profiles Distinguish Atypical From Idiopathic Parkinsonism and Track Clinical Severity Across Syndromes.

Journal of neurochemistry·2026

Same author

Peptidomic Profiling Reveals Extracellular Matrix Remodeling Signatures Discriminative of Multiple Myeloma.

Proteomics·2026

Same author

Urinary Peptidomic Signatures Predict Overall and Progression-Free Survival in Bladder Cancer.

Proteomics·2026

Same author

Urinary Collagen Peptides Predict Mortality.

Proteomics·2026

Same author

Integrative Analysis on the Urinary Proteome of Diabetic Kidney Disease, with an Emphasis on Extracellular Matrix Proteins.

International journal of molecular sciences·2026

Same author

Practical Impact of Imputation and Batch-Effect Correction for Proteomics/Peptidomics Differential-Abundance Analysis.

Proteomics·2026

Search research articles

Related Experiment Video

Updated: Oct 2, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

In Situ Peroxidase Labeling Followed by Mass-Spectrometry Reveals TIA1 Interactome.

Olga Gourdomichali^1,2, Katerina Zonke¹, Fedon-Giasin Kattan^1,3

¹Center of Basic Research, Biomedical Research Foundation, Academy of Athens, 11527 Athens, Greece.

|February 25, 2022

Summary

The TIA1 protein interacts with different partners in unstressed and stressed cells, revealing its dynamic role in RNA metabolism and cellular responses. This study maps TIA1

Keywords:

APEX2 LC-MS/MS RNA binding proteins TIA1 proteomics proximity labeling stress stress granules

More Related Videos

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Published on: March 24, 2012

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks

Published on: May 17, 2020

Related Experiment Videos

Last Updated: Oct 2, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Profiling Thiol Redox Proteome Using Isotope Tagging Mass Spectrometry

Published on: March 24, 2012

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks

TurboID-Based Proximity Labeling for In Planta Identification of Protein-Protein Interaction Networks

Published on: May 17, 2020

Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

TIA1 is a DNA/RNA binding protein crucial for RNA metabolism and stress granule assembly.
Its functions are mediated by RNA recognition motifs and a poorly characterized prion-like domain.
Understanding TIA1's protein interactions is key to elucidating its cellular roles.

Purpose of the Study:

To identify and characterize proteins interacting with TIA1 in situ under different cellular conditions.
To investigate how TIA1's protein environment changes during cellular stress.
To provide a comprehensive map of the TIA1 interactome.

Main Methods:

Fusion of enhanced ascorbate peroxidase 2 (APEX2) to TIA1 for proximity-dependent biotinylation.
Mass spectrometry to identify biotinylated proteins in the vicinity of TIA1.
Comparative analysis of TIA1 interactomes in unstressed and acutely stressed cells.

Main Results:

Identified 86 protein partners in unstressed cells and 203 in stressed cells, primarily within ribonucleoprotein complexes.
Demonstrated a significant difference in TIA1's protein partners between unstressed and stressed states.
Unstressed cells showed enrichment in mRNA metabolism processes (translation, transport, catabolism).
Stressed cells revealed broader subcellular distribution (chromosomes, mitochondria) and enrichment in splicing, translation, DNA repair, and amide metabolism.

Conclusions:

TIA1 interacts with distinct sets of proteins in different cellular states, highlighting its dynamic regulatory functions.
The study provides a detailed spatial map of TIA1 and its partners, crucial for understanding its role in RNA metabolism and stress response.
These findings lay the groundwork for further dissecting TIA1's involvement in various cellular processes.