Dünkler Alexander, Leda Marcin, Kromer Jan-Michael, Neller Joachim, Gronemeyer Thomas, Goryachev Andrew B, Johnsson Nils
Institute of Molecular Genetics and Cell Biology, Department of Biology, Ulm University, Ulm, Germany.
Centre for Synthetic and Systems Biology, Institute of Cell Biology, University of Edinburgh, Edinburgh, UK.
J Cell Biol. 2021 May 3;220(5). doi: 10.1083/jcb.202006193.
The polarisome is a cortical proteinaceous microcompartment that organizes the growth of actin filaments and the fusion of secretory vesicles in yeasts and filamentous fungi. Polarisomes are compact, spotlike structures at the growing tips of their respective cells. The molecular forces that control the form and size of this microcompartment are not known. Here we identify a complex between the polarisome subunit Pea2 and the type V Myosin Myo2 that anchors Myo2 at the cortex of yeast cells. We discovered a point mutation in the cargo-binding domain of Myo2 that impairs the interaction with Pea2 and consequently the formation and focused localization of the polarisome. Cells carrying this mutation grow round instead of elongated buds. Further experiments and biophysical modeling suggest that the interactions between polarisome-bound Myo2 motors and dynamic actin filaments spatially focus the polarisome and sustain its compact shape.
极化体是一种皮质蛋白微区室,它在酵母和丝状真菌中组织肌动蛋白丝的生长以及分泌小泡的融合。极化体是其各自细胞生长尖端处紧凑的点状结构。控制这种微区室形态和大小的分子力尚不清楚。在这里,我们鉴定出极化体亚基Pea2与V型肌球蛋白Myo2之间的一种复合物,该复合物将Myo2锚定在酵母细胞的皮质上。我们在Myo2的货物结合结构域中发现了一个点突变,该突变损害了与Pea2的相互作用,从而影响了极化体的形成和集中定位。携带这种突变的细胞长出圆形而非细长的芽。进一步的实验和生物物理建模表明,与极化体结合的Myo2马达与动态肌动蛋白丝之间的相互作用在空间上使极化体集中并维持其紧凑形状。