biostudies-literatureLee YJHHS | NIH | National Institute of General Medical SciencesUC | UCD | University of California Davis School of MedicineNIGMS NIH HHSe2303037120https://www.ebi.ac.uk/biostudies/studies/S-EPMC10104483biostudies-literatureUnknown120(15)Biomolecular condensates are nonmembranous structures that are mainly formed through liquid-liquid phase separation. Tensins are focal adhesion (FA) proteins linking the actin cytoskeleton to integrin receptors. Here, we report that GFP-tagged tensin-1 (TNS1) proteins phase-separate to form biomolecular condensates in cells. Live-cell imaging showed that new TNS1 condensates are budding from the disassembling ends of FAs, and the presence of these condensates is cell cycle dependent. TNS1 condensates dissolve immediately prior to mitosis and rapidly reappear while postmitotic daughter cells establish new FAs. TNS1 condensates contain selected FA proteins and signaling molecules such as pT308Akt but not pS473Akt, suggesting previously unknown roles of TNS1 condensates in disassembling FAs, as the storage of core FA components and the signaling intermediates.Proceedings of the National Academy of Sciences of the United States of AmericaPhase transition of tensin-1 during the focal adhesion disassembly and cell division.PMC10104483R01 GM148706GM148706the Team Research AwardLo SHYamada SLee YJfalsePhase transition of tensin-1 during the focal adhesion disassembly and cell division.Biomolecular condensates are nonmembranous structures that are mainly formed through liquid-liquid phase separation. Tensins are focal adhesion (FA) proteins linking the actin cytoskeleton to integrin receptors. Here, we report that GFP-tagged tensin-1 (TNS1) proteins phase-separate to form biomolecular condensates in cells. Live-cell imaging showed that new TNS1 condensates are budding from the disassembling ends of FAs, and the presence of these condensates is cell cycle dependent. TNS1 condensates dissolve immediately prior to mitosis and rapidly reappear while postmitotic daughter cells establish new FAs. TNS1 condensates contain selected FA proteins and signaling molecules such as pT308Akt but not pS473Akt, suggesting previously unknown roles of TNS1 condensates in disassembling FAs, as the storage of core FA components and the signaling intermediates.2023-01-01T00:00:00Z2023 Apr2025-04-05T12:13:19.354Z2025-04-05T12:13:19.354ZS-EPMC101044833701120510.1073/pnas.2303037120