PDF(Pubmed)
Abstract：
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.
摘要：
生物分子缩合物是主要通过液-液相分离形成的非膜结构。紧张素是将肌动蛋白细胞骨架与整联蛋白受体连接的粘着斑(FA)蛋白。这里,我们报道,GFP标记的张力蛋白-1(TNS1)蛋白相分离以在细胞中形成生物分子缩合物。活细胞成像显示，新的TNS1凝析油从FAs的分解端出芽，这些缩合物的存在依赖于细胞周期。TNS1冷凝物在有丝分裂之前立即溶解，并在有丝分裂后的子细胞建立新的FA时迅速重新出现。TNS1缩合物包含选定的FA蛋白和信号分子，如pT308Akt，但不包含pS473Akt，表明TNS1凝析油在分解FAs中的作用，作为核心FA组分和信号中间体的存储。
