In vivo interactome profiling by enzyme-catalyzed proximity labeling

Area of Science:

• Biochemistry
• Molecular Biology
• Proteomics

Background:

• Enzyme-catalyzed proximity labeling (PL) coupled with mass spectrometry (MS) is a powerful technique for studying protein-protein interactions and cellular organization.
• Advancements in enzymatic tags are improving the temporal and spatial resolution of PL methods.
• In vivo applications of PL are expanding, enabling studies in live animals and plants.

Purpose of the Study:

• To summarize the current state of proximity labeling-dependent interactome studies.
• To focus on in vivo applications of advanced PL techniques.
• To highlight critical considerations for successful in vivo PL experiments.

Main Methods:

• Enzyme-catalyzed proximity labeling (PL).
• Mass spectrometry (MS).
• In vivo experimental designs.

Main Results:

• PL-MS enables the study of protein-protein interaction networks in a physiological context.
• Upgraded enzymatic tags enhance catalytic efficiency and resolution.
• In vivo PL has been successfully applied to live animals and plants.

Conclusions:

• Proximity labeling is a revolutionary approach for interactome studies.
• Newer in vivo PL methods provide novel insights into protein interactomes.
• This technique has significant potential for understanding human diseases.