Characterization of the actomyosin binding interface

这个项目的目的是阐明基于肌动蛋白的运动蛋白在细胞黏附、吞噬和丝足动力学中的作用。至少四个不同肌球蛋白类别的成员似乎参与了这些过程。初步结果表明，它们的运动特性与快速骨骼肌肌球蛋白有许多相似之处，这有利于它们的生产和表征。这些肌球蛋白的不同功能特征可以与初级序列水平上的少量变化联系在一起，其详细的表征有望揭示化学-机械耦合及其调控机制的新的重要见解。特别是，我们将测试一种调节机制的意义和结构基础，通过这种调节机制，游离镁离子浓度的生理变化调节至少两个肌球蛋白的运动活动。与我们在研究单位的合作实验室一起，我们将测量单个肌球蛋白和肌球蛋白小集合产生的力，表征肌球蛋白结合伙伴，并剖析肌球蛋白VII作为黏附结构、丝状肌动蛋白和微管之间相互作用的介体所起的作用。

The aim of this project is to elucidate the function of actin-based motor proteins in cell adhesion, phagocytosis and filopodia dynamics. Members of at least four different myosin classes appear to be involved in these processes. Initial results show that their motor properties share many features with fast skeletal muscle myosins, which facilitates their production and characterization. Distinct functional features of these myosins can be linked to a small number of changes at the primary sequence level, whose detailed characterization promises to reveal new and important insights about the mechanism of chemo-mechanical coupling and its regulation. In particular, we will test the significance and structural basis of a regulatory mechanism by which physiological changes in the concentration of free Mg2+-ions modulate the motor activity of at least two of these myosins. Together with our partner laboratories in the research unit, we will measure the forces produced by individual myosins and small ensembles of myosins, characterize myosin binding partners, and dissect the role of myosin VII as mediator of interactions between adhesion structures, filamentous actin and microtubules.