In vivo interactome profiling by enzyme‐catalyzed proximity labeling

Abstract Enzyme-catalyzed proximity labeling (PL) combined with mass spectrometry (MS) has emerged as a revolutionary approach to reveal the protein-protein interaction networks, dissect complex biological processes, and characterize the subcellular proteome in a more physiological setting than befo...

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Main Authors: Yangfan Xu, Xianqun Fan, Yang Hu
Format: Article
Language:English
Published: BMC 2021-01-01
Series:Cell & Bioscience
Subjects:
Online Access:https://doi.org/10.1186/s13578-021-00542-3
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author Yangfan Xu
Xianqun Fan
Yang Hu
author_facet Yangfan Xu
Xianqun Fan
Yang Hu
author_sort Yangfan Xu
collection DOAJ
description Abstract Enzyme-catalyzed proximity labeling (PL) combined with mass spectrometry (MS) has emerged as a revolutionary approach to reveal the protein-protein interaction networks, dissect complex biological processes, and characterize the subcellular proteome in a more physiological setting than before. The enzymatic tags are being upgraded to improve temporal and spatial resolution and obtain faster catalytic dynamics and higher catalytic efficiency. In vivo application of PL integrated with other state of the art techniques has recently been adapted in live animals and plants, allowing questions to be addressed that were previously inaccessible. It is timely to summarize the current state of PL-dependent interactome studies and their potential applications. We will focus on in vivo uses of newer versions of PL and highlight critical considerations for successful in vivo PL experiments that will provide novel insights into the protein interactome in the context of human diseases.
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spelling doaj.art-dfd25dbda19249f4863a844b2edded5a2022-12-21T19:38:05ZengBMCCell & Bioscience2045-37012021-01-011111910.1186/s13578-021-00542-3In vivo interactome profiling by enzyme‐catalyzed proximity labelingYangfan Xu0Xianqun Fan1Yang Hu2Department of Ophthalmology, Stanford University School of MedicineDepartment of Ophthalmology, Ninth People’s Hospital, Shanghai JiaoTong University School of MedicineDepartment of Ophthalmology, Stanford University School of MedicineAbstract Enzyme-catalyzed proximity labeling (PL) combined with mass spectrometry (MS) has emerged as a revolutionary approach to reveal the protein-protein interaction networks, dissect complex biological processes, and characterize the subcellular proteome in a more physiological setting than before. The enzymatic tags are being upgraded to improve temporal and spatial resolution and obtain faster catalytic dynamics and higher catalytic efficiency. In vivo application of PL integrated with other state of the art techniques has recently been adapted in live animals and plants, allowing questions to be addressed that were previously inaccessible. It is timely to summarize the current state of PL-dependent interactome studies and their potential applications. We will focus on in vivo uses of newer versions of PL and highlight critical considerations for successful in vivo PL experiments that will provide novel insights into the protein interactome in the context of human diseases.https://doi.org/10.1186/s13578-021-00542-3Proximity labelingProtein interactomeAPEXBioIDTurboID
spellingShingle Yangfan Xu
Xianqun Fan
Yang Hu
In vivo interactome profiling by enzyme‐catalyzed proximity labeling
Cell & Bioscience
Proximity labeling
Protein interactome
APEX
BioID
TurboID
title In vivo interactome profiling by enzyme‐catalyzed proximity labeling
title_full In vivo interactome profiling by enzyme‐catalyzed proximity labeling
title_fullStr In vivo interactome profiling by enzyme‐catalyzed proximity labeling
title_full_unstemmed In vivo interactome profiling by enzyme‐catalyzed proximity labeling
title_short In vivo interactome profiling by enzyme‐catalyzed proximity labeling
title_sort in vivo interactome profiling by enzyme catalyzed proximity labeling
topic Proximity labeling
Protein interactome
APEX
BioID
TurboID
url https://doi.org/10.1186/s13578-021-00542-3
work_keys_str_mv AT yangfanxu invivointeractomeprofilingbyenzymecatalyzedproximitylabeling
AT xianqunfan invivointeractomeprofilingbyenzymecatalyzedproximitylabeling
AT yanghu invivointeractomeprofilingbyenzymecatalyzedproximitylabeling