INSERM U866, University of Burgundy, Dijon 21079, France.
Int J Biochem Cell Biol. 2012 Oct;44(10):1680-6. doi: 10.1016/j.biocel.2012.05.024. Epub 2012 Jun 7.
The cytoskeleton is a highly complex network of three major intracellular filaments, microfilaments (MFs), microtubules (MTs) and intermediate filaments (IFs). This network plays a key role in the control of cell shape, division, functions and interactions in animal organs and tissues. Dysregulation of the network can contribute to numerous human diseases. Although small HSPs (sHSPs) and in particular HSP27 (HSPB1) or αB-crystallin (HSPB5) display a wide range of cellular properties, they are mostly known for their ability to protect cells under stress conditions. Mutations in some sHSPs have been found to affect their ability to interact with cytoskeleton proteins, leading to IF aggregation phenotypes that mimick diseases related to disorders in IF proteins (i.e. desmin, vimentin and neuro-filaments). The aim of this review is to discuss new findings that point towards the possible involvement of IFs in the cytoprotective functions of sHSPs, both in physiological and pathological settings, including the likelihood that sHSPs such as HSPB1 may play a role during epithelial-to-mesenchymal transition (EMT) during fibrosis or cancer progression. This article is part of a Directed Issue entitled: Small HSPs in physiology and pathology.
细胞骨架是一个由三种主要的细胞内丝状结构组成的高度复杂的网络，分别是微丝（MFs）、微管（MTs）和中间丝（IFs）。这个网络在控制动物器官和组织中的细胞形状、分裂、功能和相互作用方面起着关键作用。网络的失调可能导致许多人类疾病。尽管小分子热休克蛋白（sHSPs），特别是 HSP27（HSPB1）或 αB-晶状体蛋白（HSPB5），具有广泛的细胞特性，但它们主要因其在应激条件下保护细胞的能力而闻名。已经发现一些 sHSPs 的突变会影响它们与细胞骨架蛋白相互作用的能力，导致中间丝聚集的表型，类似于与中间丝蛋白紊乱相关的疾病（即结蛋白、波形蛋白和神经丝）。本综述的目的是讨论新的发现，这些发现表明中间丝可能参与 sHSP 的细胞保护功能，无论是在生理还是病理环境下，包括 HSPB1 等 sHSP 可能在纤维化或癌症进展过程中的上皮-间充质转化（EMT）期间发挥作用的可能性。本文是题为“小分子热休克蛋白在生理和病理中的作用”的专论的一部分。
