Department of Biochemistry, Box 357350, University of Washington, Seattle, WA 98195-7350, USA.
FEBS Lett. 2013 Apr 17;587(8):1073-80. doi: 10.1016/j.febslet.2013.01.021. Epub 2013 Jan 20.
Small Heat Shock Proteins (sHSPs) are a diverse family of molecular chaperones that delay protein aggregation through interactions with non-native and aggregate-prone protein states. This function has been shown to be important to cellular viability and sHSP function/dysfunction is implicated in many diseases, including Alzheimer's and Alexander disease. Though their gene products are small, many sHSPs assemble into a distribution of large oligomeric states that undergo dynamic subunit exchange. These inherent properties present significant experimental challenges for characterizing sHSP oligomers. Of the human sHSPs, αB crystallin is a paradigm example of sHSP oligomeric properties. Advances in our understanding of sHSP structure, oligomeric distribution, and dynamics have prompted the proposal of several models for the oligomeric states of αB. The aim of this review is to highlight characteristics of αB crystallin (αB) that are key to understanding its structure and function. The current state of knowledge, existing models, and outstanding questions that remain to be addressed are presented.
小分子热休克蛋白 (sHSPs) 是一类具有多样性的分子伴侣，通过与非天然状态和易于聚集的蛋白质状态相互作用来延缓蛋白质聚集。这一功能对于细胞活力非常重要，并且 sHSP 的功能障碍与许多疾病有关，包括阿尔茨海默病和亚历山大病。尽管它们的基因产物很小，但许多 sHSP 会组装成具有动态亚基交换的大寡聚状态分布。这些固有特性给 sHSP 寡聚体的特性描述带来了重大的实验挑战。在人类 sHSPs 中，αB 晶体蛋白是 sHSP 寡聚性质的范例。对 sHSP 结构、寡聚体分布和动力学的理解的进展促使提出了几种 αB 寡聚体状态的模型。本文旨在强调 αB 晶体蛋白 (αB) 的特征，这些特征对于理解其结构和功能至关重要。介绍了当前的知识状态、现有模型以及仍需解决的悬而未决的问题。
