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

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,...

Protein-protein Interfaces

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...

You might also read

Related Articles

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

Sort by

Same author

Dementia etiology classification using NULISA plasma biomarkers and machine learning.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2026

Same author

Pre-analytical guidelines for blood and CSF Biomarkers 2025: Recommendations from the NACC ADRC Biofluid Biomarker Best Practices Workgroup.

Alzheimer's & dementia : the journal of the Alzheimer's Association·2026

Same author

Amyloid extraction from neurodegenerative disease tissues for structural studies.

Methods in enzymology·2026

Same author

Impaired motor activity in a CRISPR SCA5 L253P knock-in mouse is associated with selective β-III-spectrin subcellular redistribution in the cerebellum.

bioRxiv : the preprint server for biology·2026

Same author

Differential <i>SP4</i> expression and HSP60 abundance in buccal swabs from patients with schizophrenia.

Science advances·2026

Same author

Organoid Models of the Oral Mucosa for Precision Medicine.

Tissue engineering. Part B, Reviews·2026

Search research articles

Related Experiment Video

Updated: Sep 9, 2025

Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes

Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes

Published on: December 20, 2019

BioID2-Based Tau Interactome Reveals Novel and Known Protein Interactions Associated with Multiple Cellular Pathways.

Ahmed Atwa^1,2, Mohammed M Alhadidy^1,2, Jared Lamp^1,3

¹Department of Translational Neuroscience, College of Human Medicine, Michigan State University, Grand Rapids, Michigan 49503, United States.

Journal of Proteome Research

|September 5, 2025

Summary

This study identifies novel tau protein interactions using BioID2, revealing 324 potential interactors crucial for understanding tauopathies like Alzheimer's disease.

Keywords:

BioID2 immunoprecipitation mass spectrometry proximity ligation assay tau protein

More Related Videos

Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia

Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia

Published on: November 9, 2018

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

Published on: May 23, 2019

Related Experiment Videos

Last Updated: Sep 9, 2025

Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes

Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes

Published on: December 20, 2019

Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia

Cell-based Assay to Study Antibody-mediated Tau Clearance by Microglia

Published on: November 9, 2018

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

An In Vitro Model for Studying Tau Aggregation Using Lentiviral-mediated Transduction of Human Neurons

Published on: May 23, 2019

Area of Science:

Neuroscience
Molecular Biology
Biochemistry

Background:

Pathological tau aggregates define tauopathies, including Alzheimer's disease.
Tau protein participates in numerous physiological functions via protein interactions.
Understanding the tau interactome is key to elucidating tau's roles in health and disease.

Purpose of the Study:

To identify novel tau protein interactors using the BioID2 method.
To characterize the cellular localization and pathways of identified tau interactors.
To validate novel tau-protein interactions using orthogonal methods.

Main Methods:

Utilized in situ proximity-dependent biotinylation (BioID2) for tau interactor identification.
Applied proximity ligation assay and co-immunoprecipitation (co-IP) for interaction validation.
Analyzed interactors across various cellular compartments and biological pathways.

Main Results:

Identified 324 potential tau interactors, including cytoskeletal, nuclear, and synaptic proteins.
Validated interactions with key proteins such as MAP2, MAP6, FUS, prune1, synapsin-1, and neurabin-2.
Discovered novel tau interactors missed by traditional co-IP methods.

Conclusions:

BioID2 is a powerful tool for comprehensive tau interactome mapping.
This study expands the known tau interactome, offering new insights into tau physiology.
Findings advance understanding of tau's role in neurodegenerative diseases.