Spatiotemporal deciphering of dynamic the FUS interactome during liquid-liquid phase separation in living cells

Abstract Liquid-liquid phase separations (LLPS) are membraneless organelles driven by biomolecule assembly and are implicated in cellular physiological activities. However, spatiotemporal deciphering of the dynamic proteome in living cells during LLPS formation remains challenging. Here, we introduc...

Full description

Saved in:
Bibliographic Details
Main Authors: Sunfengda Song, Haiyang Xie, Qingwen Wang, Xinyi Sun, Jiasu Xu, Rui Chen, Yuankang Zhu, Lai Jiang, Xianting Ding
Format: Article
Language:English
Published: Nature Portfolio 2025-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-025-59457-z
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1850190577593745408
author Sunfengda Song
Haiyang Xie
Qingwen Wang
Xinyi Sun
Jiasu Xu
Rui Chen
Yuankang Zhu
Lai Jiang
Xianting Ding
author_facet Sunfengda Song
Haiyang Xie
Qingwen Wang
Xinyi Sun
Jiasu Xu
Rui Chen
Yuankang Zhu
Lai Jiang
Xianting Ding
author_sort Sunfengda Song
collection DOAJ
description Abstract Liquid-liquid phase separations (LLPS) are membraneless organelles driven by biomolecule assembly and are implicated in cellular physiological activities. However, spatiotemporal deciphering of the dynamic proteome in living cells during LLPS formation remains challenging. Here, we introduce the Composition of LLPS proteome Assembly by Proximity labeling-assisted Mass spectrometry (CLAPM). We demonstrate that CLAPM can instantaneously label and monitor the FUS interactome shifts within intracellular droplets undergoing spatiotemporal LLPS. We report 129, 182 and 822 proteins specifically present in the LLPS droplets of HeLa, HEK 293 T and neuronal cells respectively. CLAPM further categorizes spatiotemporal dynamic proteome in droplets for living neuronal cells and identifies 596 LLPS-aboriginal proteins, 226 LLPS-dependent proteins and 58 LLPS-sensitive proteins. For validation, we uncover 11 previously unknown LLPS proteins in vivo. CLAPM provides a versatile tool to decipher proteins involved in LLPS and enables the accurate characterization of dynamic proteome in living cells.
format Article
id doaj-art-6a55b1bc5a514b3b95265eac44cfe465
institution OA Journals
issn 2041-1723
language English
publishDate 2025-05-01
publisher Nature Portfolio
record_format Article
series Nature Communications
spelling doaj-art-6a55b1bc5a514b3b95265eac44cfe4652025-08-20T02:15:15ZengNature PortfolioNature Communications2041-17232025-05-0116111610.1038/s41467-025-59457-zSpatiotemporal deciphering of dynamic the FUS interactome during liquid-liquid phase separation in living cellsSunfengda Song0Haiyang Xie1Qingwen Wang2Xinyi Sun3Jiasu Xu4Rui Chen5Yuankang Zhu6Lai Jiang7Xianting Ding8Department of Anesthesiology and Surgical Intensive Care Unit, Xinhua Hospital, School of Medicine and School of Biomedical Engineering, Shanghai Jiao Tong UniversityDepartment of Anesthesiology and Surgical Intensive Care Unit, Xinhua Hospital, School of Medicine and School of Biomedical Engineering, Shanghai Jiao Tong UniversityDepartment of Anesthesiology and Surgical Intensive Care Unit, Xinhua Hospital, School of Medicine and School of Biomedical Engineering, Shanghai Jiao Tong UniversityDepartment of Anesthesiology and Surgical Intensive Care Unit, Xinhua Hospital, School of Medicine and School of Biomedical Engineering, Shanghai Jiao Tong UniversityDepartment of Anesthesiology and Surgical Intensive Care Unit, Xinhua Hospital, School of Medicine and School of Biomedical Engineering, Shanghai Jiao Tong UniversityDepartment of Anesthesiology and Surgical Intensive Care Unit, Xinhua Hospital, School of Medicine and School of Biomedical Engineering, Shanghai Jiao Tong UniversityDepartment of Anesthesiology and Surgical Intensive Care Unit, Xinhua Hospital, School of Medicine and School of Biomedical Engineering, Shanghai Jiao Tong UniversityDepartment of Anesthesiology and Surgical Intensive Care Unit, Xinhua Hospital, School of Medicine and School of Biomedical Engineering, Shanghai Jiao Tong UniversityDepartment of Anesthesiology and Surgical Intensive Care Unit, Xinhua Hospital, School of Medicine and School of Biomedical Engineering, Shanghai Jiao Tong UniversityAbstract Liquid-liquid phase separations (LLPS) are membraneless organelles driven by biomolecule assembly and are implicated in cellular physiological activities. However, spatiotemporal deciphering of the dynamic proteome in living cells during LLPS formation remains challenging. Here, we introduce the Composition of LLPS proteome Assembly by Proximity labeling-assisted Mass spectrometry (CLAPM). We demonstrate that CLAPM can instantaneously label and monitor the FUS interactome shifts within intracellular droplets undergoing spatiotemporal LLPS. We report 129, 182 and 822 proteins specifically present in the LLPS droplets of HeLa, HEK 293 T and neuronal cells respectively. CLAPM further categorizes spatiotemporal dynamic proteome in droplets for living neuronal cells and identifies 596 LLPS-aboriginal proteins, 226 LLPS-dependent proteins and 58 LLPS-sensitive proteins. For validation, we uncover 11 previously unknown LLPS proteins in vivo. CLAPM provides a versatile tool to decipher proteins involved in LLPS and enables the accurate characterization of dynamic proteome in living cells.https://doi.org/10.1038/s41467-025-59457-z
spellingShingle Sunfengda Song
Haiyang Xie
Qingwen Wang
Xinyi Sun
Jiasu Xu
Rui Chen
Yuankang Zhu
Lai Jiang
Xianting Ding
Spatiotemporal deciphering of dynamic the FUS interactome during liquid-liquid phase separation in living cells
Nature Communications
title Spatiotemporal deciphering of dynamic the FUS interactome during liquid-liquid phase separation in living cells
title_full Spatiotemporal deciphering of dynamic the FUS interactome during liquid-liquid phase separation in living cells
title_fullStr Spatiotemporal deciphering of dynamic the FUS interactome during liquid-liquid phase separation in living cells
title_full_unstemmed Spatiotemporal deciphering of dynamic the FUS interactome during liquid-liquid phase separation in living cells
title_short Spatiotemporal deciphering of dynamic the FUS interactome during liquid-liquid phase separation in living cells
title_sort spatiotemporal deciphering of dynamic the fus interactome during liquid liquid phase separation in living cells
url https://doi.org/10.1038/s41467-025-59457-z
work_keys_str_mv AT sunfengdasong spatiotemporaldecipheringofdynamicthefusinteractomeduringliquidliquidphaseseparationinlivingcells
AT haiyangxie spatiotemporaldecipheringofdynamicthefusinteractomeduringliquidliquidphaseseparationinlivingcells
AT qingwenwang spatiotemporaldecipheringofdynamicthefusinteractomeduringliquidliquidphaseseparationinlivingcells
AT xinyisun spatiotemporaldecipheringofdynamicthefusinteractomeduringliquidliquidphaseseparationinlivingcells
AT jiasuxu spatiotemporaldecipheringofdynamicthefusinteractomeduringliquidliquidphaseseparationinlivingcells
AT ruichen spatiotemporaldecipheringofdynamicthefusinteractomeduringliquidliquidphaseseparationinlivingcells
AT yuankangzhu spatiotemporaldecipheringofdynamicthefusinteractomeduringliquidliquidphaseseparationinlivingcells
AT laijiang spatiotemporaldecipheringofdynamicthefusinteractomeduringliquidliquidphaseseparationinlivingcells
AT xiantingding spatiotemporaldecipheringofdynamicthefusinteractomeduringliquidliquidphaseseparationinlivingcells