帕西林
生物
焦点粘着
细胞生物学
整合素
跨膜蛋白
信号转导
支架蛋白
化学
受体
生物化学
细胞
作者
Peigang Liang,Ying Wu,Shanyuan Zheng,J Zhang,Shuo Yang,Jinfang Wang,Suibin Ma,Mengjun Zhang,Zhuang Gu,Qingfeng Liu,Wen-Xue Jiang,Qiong Xing,Bo Wang
标识
DOI:10.1083/jcb.202209027
摘要
Focal adhesions (FAs) are transmembrane protein assemblies mediating cell–matrix connection. Although protein liquid–liquid phase separation (LLPS) has been tied to the organization and dynamics of FAs, the underlying mechanisms remain unclear. Here, we experimentally tune the LLPS of PXN/Paxillin, an essential scaffold protein of FAs, by utilizing a light-inducible Cry2 system in different cell types. In addition to nucleating FA components, light-triggered PXN LLPS potently activates integrin signaling and subsequently accelerates cell spreading. In contrast to the homotypic interaction-driven LLPS of PXN in vitro, PXN condensates in cells are associated with the plasma membrane and modulated by actomyosin contraction and client proteins of FAs. Interestingly, non-specific weak intermolecular interactions synergize with specific molecular interactions to mediate the multicomponent condensation of PXN and are efficient in promoting FA assembly and integrin signaling. Thus, our data establish an active role of the PXN phase transition into a condensed membrane-associated compartment in promoting the assembly/maturation of FAs.
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