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Management of cytoskeleton architecture by molecular chaperones and immunophilins

机译：分子伴侣和免疫亲和素对细胞骨架结构的管理

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Cytoskeletal structure is continually remodeled to accommodate normal cell growth and to respond to pathophysiological cues. As a consequence, several cytoskeleton-interacting proteins become involved in a variety of cellular processes such as cell growth and division, cell movement, vesicle transportation, cellular organelle location and function, localization and distribution of membrane receptors, and cell-cell communication. Molecular chaperones and immunophilins are counted among the most important proteins that interact closely with the cytoskeleton network, in particular with microtubules and microtubule-associated factors. In several situations, heat-shock proteins and immunophilins work together as a functionally active heterocomplex, although both types of proteins also show independent actions. In circumstances where homeostasis is affected by environmental stresses or due to genetic alterations, chaperone proteins help to stabilize the system. Molecular chaperones facilitate the assembly, disassembly and/or folding/refolding of cytoskeletal proteins, so they prevent aberrant protein aggregation. Nonetheless, the roles of heat-shock proteins and immunophilins are not only limited to solve abnormal situations, but they also have an active participation during the normal differentiation process of the cell and are key factors for many structural and functional rearrangements during this course of action. Cytoskeleton modifications leading to altered localization of nuclear factors may result in loss- or gain-of-function of such factors, which affects the cell cycle and cell development. Therefore, cytoskeletal components are attractive therapeutic targets, particularly microtubules, to prevent pathological situations such as rapidly dividing tumor cells or to favor the process of cell differentiation in other cases. In this review we will address some classical and novel aspects of key regulatory functions of heat-shock proteins and immunophilins as housekeeping factors of the cytoskeletal network.
机译：细胞骨架结构不断进行改造，以适应正常的细胞生长并响应病理生理学提示。结果，几种细胞骨架相互作用的蛋白质参与了各种细胞过程，例如细胞生长和分裂，细胞运动，囊泡运输，细胞器位置和功能，膜受体的定位和分布以及细胞间的通讯。分子伴侣和免疫亲和素被认为是与细胞骨架网络，特别是与微管和微管相关因子紧密相互作用的最重要的蛋白质之一。在几种情况下，热激蛋白和亲免蛋白可以一起发挥功能活性异源复合物的作用，尽管两种类型的蛋白也显示出独立的作用。在环境压力或由于遗传改变影响体内平衡的情况下，伴侣蛋白有助于稳定系统。分子伴侣可促进细胞骨架蛋白的组装，拆卸和/或折叠/再折叠，因此它们可防止异常的蛋白聚集。尽管如此，热休克蛋白和亲免蛋白的作用不仅限于解决异常情况，而且在细胞正常分化过程中也具有积极参与作用，并且是此过程中许多结构和功能重排的关键因素。导致核因子定位改变的细胞骨架修饰可能导致此类因子丧失功能或获得功能，从而影响细胞周期和细胞发育。因此，细胞骨架组分是有吸引力的治疗靶标，特别是微管，以防止诸如快速分裂肿瘤细胞之类的病理情况或在其他情况下有利于细胞分化过程。在这篇综述中，我们将探讨热休克蛋白和亲免蛋白作为细胞骨架网络管家因子的关键调控功能的一些经典和新颖方面。

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