生物
细胞生物学
内吞作用
内吞循环
肌动蛋白
网格蛋白
肌动蛋白重塑
胞饮病
肌动蛋白结合蛋白
肌动蛋白细胞骨架
细胞骨架
生物化学
受体
细胞
作者
Andrew K. Lamb,Andres Fernandez,Abdunaser Eadaim,Katelyn Johnson,Santiago Di Pietro
标识
DOI:10.1083/jcb.202306154
摘要
Clathrin-mediated endocytosis depends on polymerization of a branched actin network to provide force for membrane invagination. A key regulator in branched actin network formation is actin capping protein (CP), which binds to the barbed end of actin filaments to prevent the addition or loss of actin subunits. CP was thought to stochastically bind actin filaments, but recent evidence shows CP is regulated by a group of proteins containing CP-interacting (CPI) motifs. Importantly, how CPI motif proteins function together to regulate CP is poorly understood. Here, we show Aim21 and Bsp1 work synergistically to recruit CP to the endocytic actin network in budding yeast through their CPI motifs, which also allosterically modulate capping strength. In contrast, twinfilin works downstream of CP recruitment, regulating the turnover of CP through its CPI motif and a non-allosteric mechanism. Collectively, our findings reveal how three CPI motif proteins work together to regulate CP in a stepwise fashion during endocytosis.
科研通智能强力驱动
Strongly Powered by AbleSci AI