Department of Cell and Developmental Biology, University of Illinois, Urbana-Champaign, Urbana, Illinois 61801.
Department Chemie, Technische Universität München, Garching 85748, Germany.
Cold Spring Harb Perspect Biol. 2019 Oct 1;11(10):a034009. doi: 10.1101/cshperspect.a034009.
Maintenance of a healthy and functional proteome in all cellular compartments is critical to cell and organismal homeostasis. Yet, our understanding of the proteostasis process within the nucleus is limited. Here, we discuss the identified roles of the major molecular chaperones Hsp90, Hsp70, and Hsp60 with client proteins working in diverse DNA-associated pathways. The unique challenges facing proteins in the nucleus are considered as well as the conserved features of the molecular chaperone system in facilitating DNA-linked processes. As nuclear protein inclusions are a common feature of protein-aggregation diseases (e.g., neurodegeneration), a better understanding of nuclear proteostasis is warranted.
维持所有细胞区室中健康和功能正常的蛋白质组对于细胞和生物体的动态平衡至关重要。然而，我们对核内蛋白质稳态过程的理解是有限的。在这里，我们讨论了主要分子伴侣 Hsp90、Hsp70 和 Hsp60 与在不同 DNA 相关途径中发挥作用的客户蛋白的已确定作用。还考虑了核内蛋白面临的独特挑战以及分子伴侣系统在促进 DNA 相关过程中的保守特征。由于核蛋白包涵体是蛋白质聚集疾病（如神经退行性疾病）的一个常见特征，因此有必要更好地了解核蛋白质稳态。
