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Phase 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 biomolec...

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Detalles Bibliográficos
Autores principales: Lee, Yuh-Ru Julie, Yamada, Soichiro, Lo, Su Hao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: National Academy of Sciences 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10104483/
https://www.ncbi.nlm.nih.gov/pubmed/37011205
http://dx.doi.org/10.1073/pnas.2303037120
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author Lee, Yuh-Ru Julie
Yamada, Soichiro
Lo, Su Hao
author_facet Lee, Yuh-Ru Julie
Yamada, Soichiro
Lo, Su Hao
author_sort Lee, Yuh-Ru Julie
collection PubMed
description 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.
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spelling pubmed-101044832023-04-15 Phase transition of tensin-1 during the focal adhesion disassembly and cell division Lee, Yuh-Ru Julie Yamada, Soichiro Lo, Su Hao Proc Natl Acad Sci U S A Biological Sciences 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. National Academy of Sciences 2023-04-03 2023-04-11 /pmc/articles/PMC10104483/ /pubmed/37011205 http://dx.doi.org/10.1073/pnas.2303037120 Text en Copyright © 2023 the Author(s). Published by PNAS. https://creativecommons.org/licenses/by-nc-nd/4.0/This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) .
spellingShingle Biological Sciences
Lee, Yuh-Ru Julie
Yamada, Soichiro
Lo, Su Hao
Phase transition of tensin-1 during the focal adhesion disassembly and cell division
title Phase transition of tensin-1 during the focal adhesion disassembly and cell division
title_full Phase transition of tensin-1 during the focal adhesion disassembly and cell division
title_fullStr Phase transition of tensin-1 during the focal adhesion disassembly and cell division
title_full_unstemmed Phase transition of tensin-1 during the focal adhesion disassembly and cell division
title_short Phase transition of tensin-1 during the focal adhesion disassembly and cell division
title_sort phase transition of tensin-1 during the focal adhesion disassembly and cell division
topic Biological Sciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10104483/
https://www.ncbi.nlm.nih.gov/pubmed/37011205
http://dx.doi.org/10.1073/pnas.2303037120
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