Paxillin phase separation promotes focal adhesion assembly and integrin signaling

• DOI: 10.1083/jcb.202209027
• Publication Date: 2024-03-11T12:57:52Z
• Authors: Peigang Liang; Yuchen Wu; Shanyuan Zheng; Jiaqi Zhang; Shuo Yang; Jinfang Wang; Suibin Ma; Mengjun Zhang; Zhuang Gu; Qingfeng Liu; Wenxue Jiang; Qiong Xing; Bo Wang
• Keywords: Paxillin

Focal adhesions (FAs) are transmembrane protein assemblies mediating cell–matrix connection. Although liquid–liquid phase separation (LLPS) has been tied to the organization and dynamics of FAs, underlying mechanisms remain unclear. Here, we experimentally tune LLPS PXN/Paxillin, an essential scaffold by utilizing a light-inducible Cry2 system in different cell types. In addition nucleating FA components, light-triggered PXN potently activates integrin signaling subsequently accelerates spreading. contrast homotypic interaction-driven vitro, condensates cells associated with plasma membrane modulated actomyosin contraction client proteins FAs. Interestingly, non-specific weak intermolecular interactions synergize specific molecular mediate multicomponent condensation efficient promoting assembly signaling. Thus, our data establish active role transition into condensed membrane-associated compartment assembly/maturation