Department of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37205, USA.
Trends Cell Biol. 2010 Jul;20(7):418-26. doi: 10.1016/j.tcb.2010.04.004. Epub 2010 May 12.
Class 1 myosins are small motor proteins with the ability to simultaneously bind to actin filaments and cellular membranes. Given their ability to generate mechanical force, and their high prevalence in many cell types, these molecules are well positioned to carry out several important biological functions at the interface of membrane and the actin cytoskeleton. Indeed, recent studies implicate these motors in endocytosis, exocytosis, release of extracellular vesicles, and the regulation of tension between membrane and the cytoskeleton. Many class 1 myosins also exhibit a load-dependent mechano-chemical cycle that enables them to maintain tension for long periods of time without hydrolyzing ATP. These properties put myosins-1 in a unique position to regulate dynamic membrane-cytoskeleton interactions and respond to physical forces during these events.
I 类肌球蛋白是能够同时结合肌动蛋白丝和细胞膜的小型运动蛋白。鉴于它们产生机械力的能力,以及它们在许多细胞类型中的高普遍性,这些分子非常适合在膜和肌动蛋白细胞骨架的界面上执行几个重要的生物学功能。事实上,最近的研究表明这些分子参与了内吞作用、胞吐作用、细胞外囊泡的释放以及膜和细胞骨架之间张力的调节。许多 I 类肌球蛋白也表现出一种负载依赖的机械化学循环,使它们能够在不水解 ATP 的情况下长时间维持张力。这些特性使肌球蛋白-1 能够独特地调节动态膜-细胞骨架相互作用,并在这些事件中响应物理力。