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OrthoID: profiling dynamic proteomes through time and space using mutually orthogonal chemical toolsopen access

Authors
Lee, AraSung, GihyunShin, SangheeLee, Song-YiSim, JaehwanNhung, Truong Thi MyNghi, Tran DiemPark, Sang KiSathieshkumar, Ponnusamy PonKang, ImkyeungMun, Ji YoungKim, Jong-SeoRhee, Hyun-WooPark, Kyeng MinKim, Kimoon
Issue Date
Feb-2024
Publisher
Nature Publishing Group
Citation
Nature Communications, v.15, no.1
Journal Title
Nature Communications
Volume
15
Number
1
URI
http://scholarworks.bwise.kr/kbri/handle/2023.sw.kbri/1161
DOI
10.1038/s41467-024-46034-z
ISSN
2041-1723
Abstract
Identifying proteins at organelle contact sites, such as mitochondria-associated endoplasmic reticulum membranes (MAM), is essential for understanding vital cellular processes, yet challenging due to their dynamic nature. Here we report "OrthoID", a proteomic method utilizing engineered enzymes, TurboID and APEX2, for the biotinylation (Bt) and adamantylation (Ad) of proteins close to the mitochondria and endoplasmic reticulum (ER), respectively, in conjunction with high-affinity binding pairs, streptavidin-biotin (SA-Bt) and cucurbit[7]uril-adamantane (CB[7]-Ad), for selective orthogonal enrichment of Bt- and Ad-labeled proteins. This approach effectively identifies protein candidates associated with the ER-mitochondria contact, including LRC59, whose roles at the contact site were-to the best of our knowledge-previously unknown, and tracks multiple protein sets undergoing structural and locational changes at MAM during mitophagy. These findings demonstrate that OrthoID could be a powerful proteomics tool for the identification and analysis of spatiotemporal proteins at organelle contact sites and revealing their dynamic behaviors in vital cellular processes.,Proteomics at the organelle contact site remains challenging due to the spatial and temporal dynamics of proteins. Here, the authors developed OrthoID, a mutually orthogonal dual enzymatic proteomics approach to explore the proteome at the contact site of the endoplasmic reticulum and mitochondria.,
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