Mechanisms of formin-mediated actin assembly and dynamics.
Mechanisms of formin-mediated actin assembly and dynamics.
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DOI：
10.1007/s12551-018-0468-6
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发表时间：
2018-12-01
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通讯作者：
Courtemanche, Naomi
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作者：
Courtemanche, Naomi
细胞的生存需要对肌动蛋白细胞骨架动力学的严格调控。不同的成核促进因子家族使细丝核能够快速组装，这些细丝核延长并被结合到不同的、专门的肌动蛋白结构中。除了促进细丝成核外，Forin蛋白家族还指导未分枝的肌动蛋白细丝的延长。通过高度保守的二聚体福尔敏同源(FH)2结构域的连续带刺末端结合，实现了福尔丁与生长的丝状末端的进行性结合。在与FH1结构域和C末端尾部区域的合作中，FH2二聚体介导肌动蛋白亚单位的增加，其速度可以显著超过自发组装的速度。在这里，我回顾了最近的生物物理、结构和计算研究，这些研究提供了对Forin介导的肌动蛋白组装和动力学机制的洞察。
Cellular viability requires tight regulation of actin cytoskeletal dynamics. Distinct families of nucleation-promoting factors enable the rapid assembly of filament nuclei that elongate and are incorporated into diverse and specialized actin-based structures. In addition to promoting filament nucleation, the formin family of proteins directs the elongation of unbranched actin filaments. Processive association of formins with growing filament ends is achieved through continuous barbed end binding of the highly conserved, dimeric formin homology (FH) 2 domain. In cooperation with the FH1 domain and C-terminal tail region, FH2 dimers mediate actin subunit addition at speeds that can dramatically exceed the rate of spontaneous assembly. Here, I review recent biophysical, structural, and computational studies that have provided insight into the mechanisms of formin-mediated actin assembly and dynamics.