Grose Julianne H, Langston Kelsey, Wang Xiaohui, Squires Shayne, Mustafi Soumyajit Banerjee, Hayes Whitney, Neubert Jonathan, Fischer Susan K, Fasano Matthew, Saunders Gina Moore, Dai Qiang, Christians Elisabeth, Lewandowski E Douglas, Ping Peipei, Benjamin Ivor J
Microbiology and Molecular Biology Department, Brigham Young University, Provo, UT, 84602, United States of America.
Laboratory of Cardiac Disease, Redox Signaling and Cell Regeneration, Division of Cardiology, University of Utah School of Medicine, Salt Lake City, UT, 84132, United States of America.
PLoS One. 2015 Oct 14;10(10):e0133994. doi: 10.1371/journal.pone.0133994. eCollection 2015.
Small Heat Shock Proteins (sHSPs) are molecular chaperones that transiently interact with other proteins, thereby assisting with quality control of proper protein folding and/or degradation. They are also recruited to protect cells from a variety of stresses in response to extreme heat, heavy metals, and oxidative-reductive stress. Although ten human sHSPs have been identified, their likely diverse biological functions remain an enigma in health and disease, and much less is known about non-redundant roles in selective cells and tissues. Herein, we set out to comprehensively characterize the cardiac-restricted Heat Shock Protein B-2 (HspB2), which exhibited ischemic cardioprotection in transgenic overexpressing mice including reduced infarct size and maintenance of ATP levels. Global yeast two-hybrid analysis using HspB2 (bait) and a human cardiac library (prey) coupled with co-immunoprecipitation studies for mitochondrial target validation revealed the first HspB2 "cardiac interactome" to contain many myofibril and mitochondrial-binding partners consistent with the overexpression phenotype. This interactome has been submitted to the Biological General Repository for Interaction Datasets (BioGRID). A related sHSP chaperone HspB5 had only partially overlapping binding partners, supporting specificity of the interactome as well as non-redundant roles reported for these sHSPs. Evidence that the cardiac yeast two-hybrid HspB2 interactome targets resident mitochondrial client proteins is consistent with the role of HspB2 in maintaining ATP levels and suggests new chaperone-dependent functions for metabolic homeostasis. One of the HspB2 targets, glyceraldehyde 3-phosphate dehydrogenase (GAPDH), has reported roles in HspB2 associated phenotypes including cardiac ATP production, mitochondrial function, and apoptosis, and was validated as a potential client protein of HspB2 through chaperone assays. From the clientele and phenotypes identified herein, it is tempting to speculate that small molecule activators of HspB2 might be deployed to mitigate mitochondrial related diseases such as cardiomyopathy and neurodegenerative disease.
小分子热休克蛋白(sHSPs)是一类分子伴侣,它们与其他蛋白质短暂相互作用,从而协助对蛋白质正确折叠和/或降解进行质量控制。它们还被募集来保护细胞免受多种应激,如极端高温、重金属以及氧化还原应激。尽管已鉴定出十种人类sHSPs,但它们在健康和疾病中可能具有的多种生物学功能仍是个谜,而且对于它们在特定细胞和组织中的非冗余作用了解更少。在此,我们着手全面表征心脏特异性的热休克蛋白B-2(HspB2),该蛋白在转基因过表达小鼠中表现出缺血性心脏保护作用,包括梗死面积减小和ATP水平维持。使用HspB2(诱饵)和人类心脏文库(猎物)进行的全基因组酵母双杂交分析,以及用于线粒体靶点验证的免疫共沉淀研究,揭示了首个HspB2“心脏相互作用组”,其中包含许多与过表达表型一致的肌原纤维和线粒体结合伴侣。这个相互作用组已提交至生物相互作用数据集通用存储库(BioGRID)。相关的sHSP伴侣蛋白HspB5只有部分重叠的结合伴侣,这支持了相互作用组的特异性以及这些sHSPs所报道的非冗余作用。心脏酵母双杂交HspB2相互作用组靶向驻留线粒体客户蛋白的证据与HspB2在维持ATP水平中的作用一致,并提示了代谢稳态中新的伴侣蛋白依赖性功能。HspB2的一个靶点,即甘油醛-3-磷酸脱氢酶(GAPDH),在与HspB2相关的表型中发挥作用,包括心脏ATP生成、线粒体功能和细胞凋亡,并通过伴侣蛋白分析被验证为HspB2的潜在客户蛋白。从本文鉴定的客户蛋白和表型推测,HspB2的小分子激活剂可能被用于减轻线粒体相关疾病,如心肌病和神经退行性疾病。