Pupylation-Based Proximity Labeling Unravels a Comprehensive Protein and Phosphoprotein Interactome of the Arabidopsis TOR Complex. Zheng, S., Blaschek, L., Pottier, D., Dijkhof, L. R. H., Özmen, B., Lim, P. K., Tan, Q. W., Mutwil, M., Hauser, A. S., & Persson, S. Advanced Science, 12(19):2414496, 2025. _eprint: https://advanced.onlinelibrary.wiley.com/doi/pdf/10.1002/advs.202414496![Pupylation-Based Proximity Labeling Unravels a Comprehensive Protein and Phosphoprotein Interactome of the Arabidopsis TOR Complex [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Target of rapamycin (TOR) is a signaling hub that integrates developmental, hormonal, and environmental signals to optimize carbon allocation and plant growth. In plant cells, TOR acts together with the proteins LST8-1 and RAPTOR1 to form a core TOR complex (TORC). While these proteins comprise a functional TORC, they engage with many other proteins to ensure precise signal outputs. Although TORC interactions have attracted significant attention in the recent past, large parts of the interactome are still unknown. In this resource study, PUP-IT is adapted, a fully endogenously expressed protein proximity labeling toolbox, to map TORC protein–protein interactions using the core set of TORC as baits. It is outlined how this interactome is differentially phosphorylated during changes in carbon availability, uncovering putative direct TOR kinase targets. An AlphaFold-Multimer approach is further used to validate many interactors, thus outlining a comprehensive TORC interactome that includes over a hundred new candidate interactors and provides an invaluable resource to the plant cell signaling community.
@article{zheng_pupylation-based_2025,
title = {Pupylation-{Based} {Proximity} {Labeling} {Unravels} a {Comprehensive} {Protein} and {Phosphoprotein} {Interactome} of the {Arabidopsis} {TOR} {Complex}},
volume = {12},
copyright = {© 2025 The Author(s). Advanced Science published by Wiley-VCH GmbH},
issn = {2198-3844},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/advs.202414496},
doi = {10.1002/advs.202414496},
abstract = {Target of rapamycin (TOR) is a signaling hub that integrates developmental, hormonal, and environmental signals to optimize carbon allocation and plant growth. In plant cells, TOR acts together with the proteins LST8-1 and RAPTOR1 to form a core TOR complex (TORC). While these proteins comprise a functional TORC, they engage with many other proteins to ensure precise signal outputs. Although TORC interactions have attracted significant attention in the recent past, large parts of the interactome are still unknown. In this resource study, PUP-IT is adapted, a fully endogenously expressed protein proximity labeling toolbox, to map TORC protein–protein interactions using the core set of TORC as baits. It is outlined how this interactome is differentially phosphorylated during changes in carbon availability, uncovering putative direct TOR kinase targets. An AlphaFold-Multimer approach is further used to validate many interactors, thus outlining a comprehensive TORC interactome that includes over a hundred new candidate interactors and provides an invaluable resource to the plant cell signaling community.},
language = {en},
number = {19},
urldate = {2026-01-30},
journal = {Advanced Science},
author = {Zheng, Shuai and Blaschek, Leonard and Pottier, Delphine and Dijkhof, Luuk Robin Hoegen and Özmen, Beyza and Lim, Peng Ken and Tan, Qiao Wen and Mutwil, Marek and Hauser, Alexander Sebastian and Persson, Staffan},
year = {2025},
note = {\_eprint: https://advanced.onlinelibrary.wiley.com/doi/pdf/10.1002/advs.202414496},
keywords = {AlphaFold, PUP-IT, proximity labeling, sugar signaling, target of rapamycin},
pages = {2414496},
}
Downloads: 0
{"_id":"fJJBncJpaJvp8t74H","bibbaseid":"zheng-blaschek-pottier-dijkhof-zmen-lim-tan-mutwil-etal-pupylationbasedproximitylabelingunravelsacomprehensiveproteinandphosphoproteininteractomeofthearabidopsistorcomplex-2025","author_short":["Zheng, S.","Blaschek, L.","Pottier, D.","Dijkhof, L. R. H.","Özmen, B.","Lim, P. K.","Tan, Q. W.","Mutwil, M.","Hauser, A. S.","Persson, S."],"bibdata":{"bibtype":"article","type":"article","title":"Pupylation-Based Proximity Labeling Unravels a Comprehensive Protein and Phosphoprotein Interactome of the Arabidopsis TOR Complex","volume":"12","copyright":"© 2025 The Author(s). Advanced Science published by Wiley-VCH GmbH","issn":"2198-3844","url":"https://onlinelibrary.wiley.com/doi/abs/10.1002/advs.202414496","doi":"10.1002/advs.202414496","abstract":"Target of rapamycin (TOR) is a signaling hub that integrates developmental, hormonal, and environmental signals to optimize carbon allocation and plant growth. In plant cells, TOR acts together with the proteins LST8-1 and RAPTOR1 to form a core TOR complex (TORC). While these proteins comprise a functional TORC, they engage with many other proteins to ensure precise signal outputs. Although TORC interactions have attracted significant attention in the recent past, large parts of the interactome are still unknown. In this resource study, PUP-IT is adapted, a fully endogenously expressed protein proximity labeling toolbox, to map TORC protein–protein interactions using the core set of TORC as baits. It is outlined how this interactome is differentially phosphorylated during changes in carbon availability, uncovering putative direct TOR kinase targets. An AlphaFold-Multimer approach is further used to validate many interactors, thus outlining a comprehensive TORC interactome that includes over a hundred new candidate interactors and provides an invaluable resource to the plant cell signaling community.","language":"en","number":"19","urldate":"2026-01-30","journal":"Advanced Science","author":[{"propositions":[],"lastnames":["Zheng"],"firstnames":["Shuai"],"suffixes":[]},{"propositions":[],"lastnames":["Blaschek"],"firstnames":["Leonard"],"suffixes":[]},{"propositions":[],"lastnames":["Pottier"],"firstnames":["Delphine"],"suffixes":[]},{"propositions":[],"lastnames":["Dijkhof"],"firstnames":["Luuk","Robin","Hoegen"],"suffixes":[]},{"propositions":[],"lastnames":["Özmen"],"firstnames":["Beyza"],"suffixes":[]},{"propositions":[],"lastnames":["Lim"],"firstnames":["Peng","Ken"],"suffixes":[]},{"propositions":[],"lastnames":["Tan"],"firstnames":["Qiao","Wen"],"suffixes":[]},{"propositions":[],"lastnames":["Mutwil"],"firstnames":["Marek"],"suffixes":[]},{"propositions":[],"lastnames":["Hauser"],"firstnames":["Alexander","Sebastian"],"suffixes":[]},{"propositions":[],"lastnames":["Persson"],"firstnames":["Staffan"],"suffixes":[]}],"year":"2025","note":"_eprint: https://advanced.onlinelibrary.wiley.com/doi/pdf/10.1002/advs.202414496","keywords":"AlphaFold, PUP-IT, proximity labeling, sugar signaling, target of rapamycin","pages":"2414496","bibtex":"@article{zheng_pupylation-based_2025,\n\ttitle = {Pupylation-{Based} {Proximity} {Labeling} {Unravels} a {Comprehensive} {Protein} and {Phosphoprotein} {Interactome} of the {Arabidopsis} {TOR} {Complex}},\n\tvolume = {12},\n\tcopyright = {© 2025 The Author(s). Advanced Science published by Wiley-VCH GmbH},\n\tissn = {2198-3844},\n\turl = {https://onlinelibrary.wiley.com/doi/abs/10.1002/advs.202414496},\n\tdoi = {10.1002/advs.202414496},\n\tabstract = {Target of rapamycin (TOR) is a signaling hub that integrates developmental, hormonal, and environmental signals to optimize carbon allocation and plant growth. In plant cells, TOR acts together with the proteins LST8-1 and RAPTOR1 to form a core TOR complex (TORC). While these proteins comprise a functional TORC, they engage with many other proteins to ensure precise signal outputs. Although TORC interactions have attracted significant attention in the recent past, large parts of the interactome are still unknown. In this resource study, PUP-IT is adapted, a fully endogenously expressed protein proximity labeling toolbox, to map TORC protein–protein interactions using the core set of TORC as baits. It is outlined how this interactome is differentially phosphorylated during changes in carbon availability, uncovering putative direct TOR kinase targets. An AlphaFold-Multimer approach is further used to validate many interactors, thus outlining a comprehensive TORC interactome that includes over a hundred new candidate interactors and provides an invaluable resource to the plant cell signaling community.},\n\tlanguage = {en},\n\tnumber = {19},\n\turldate = {2026-01-30},\n\tjournal = {Advanced Science},\n\tauthor = {Zheng, Shuai and Blaschek, Leonard and Pottier, Delphine and Dijkhof, Luuk Robin Hoegen and Özmen, Beyza and Lim, Peng Ken and Tan, Qiao Wen and Mutwil, Marek and Hauser, Alexander Sebastian and Persson, Staffan},\n\tyear = {2025},\n\tnote = {\\_eprint: https://advanced.onlinelibrary.wiley.com/doi/pdf/10.1002/advs.202414496},\n\tkeywords = {AlphaFold, PUP-IT, proximity labeling, sugar signaling, target of rapamycin},\n\tpages = {2414496},\n}\n\n\n\n","author_short":["Zheng, S.","Blaschek, L.","Pottier, D.","Dijkhof, L. R. H.","Özmen, B.","Lim, P. K.","Tan, Q. W.","Mutwil, M.","Hauser, A. S.","Persson, S."],"key":"zheng_pupylation-based_2025","id":"zheng_pupylation-based_2025","bibbaseid":"zheng-blaschek-pottier-dijkhof-zmen-lim-tan-mutwil-etal-pupylationbasedproximitylabelingunravelsacomprehensiveproteinandphosphoproteininteractomeofthearabidopsistorcomplex-2025","role":"author","urls":{"Paper":"https://onlinelibrary.wiley.com/doi/abs/10.1002/advs.202414496"},"keyword":["AlphaFold","PUP-IT","proximity labeling","sugar signaling","target of rapamycin"],"metadata":{"authorlinks":{}}},"bibtype":"article","biburl":"https://bibbase.org/zotero/upscpub","dataSources":["9cGcv2t8pRzC92kzs"],"keywords":["alphafold","pup-it","proximity labeling","sugar signaling","target of rapamycin"],"search_terms":["pupylation","based","proximity","labeling","unravels","comprehensive","protein","phosphoprotein","interactome","arabidopsis","tor","complex","zheng","blaschek","pottier","dijkhof","özmen","lim","tan","mutwil","hauser","persson"],"title":"Pupylation-Based Proximity Labeling Unravels a Comprehensive Protein and Phosphoprotein Interactome of the Arabidopsis TOR Complex","year":2025}