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在机械压力下维持蛋白质平衡。

Maintaining proteostasis under mechanical stress.

机构信息

Institute for Cell Biology, Rheinische Friedrich-Wilhelms University Bonn, Bonn, Germany.

Department II of Internal Medicine and Center for Molecular Medicine Cologne (CMMC), University of Cologne, Cologne, Germany.

出版信息

EMBO Rep. 2021 Aug 4;22(8):e52507. doi: 10.15252/embr.202152507. Epub 2021 Jul 26.

DOI:10.15252/embr.202152507
PMID:34309183
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8339670/
Abstract

Cell survival, tissue integrity and organismal health depend on the ability to maintain functional protein networks even under conditions that threaten protein integrity. Protection against such stress conditions involves the adaptation of folding and degradation machineries, which help to preserve the protein network by facilitating the refolding or disposal of damaged proteins. In multicellular organisms, cells are permanently exposed to stress resulting from mechanical forces. Yet, for long time mechanical stress was not recognized as a primary stressor that perturbs protein structure and threatens proteome integrity. The identification and characterization of protein folding and degradation systems, which handle force-unfolded proteins, marks a turning point in this regard. It has become apparent that mechanical stress protection operates during cell differentiation, adhesion and migration and is essential for maintaining tissues such as skeletal muscle, heart and kidney as well as the immune system. Here, we provide an overview of recent advances in our understanding of mechanical stress protection.

摘要

细胞的存活、组织的完整性和生物体的健康依赖于在威胁蛋白质完整性的条件下维持功能蛋白网络的能力。针对这种应激条件的保护涉及到折叠和降解机制的适应,这些机制通过促进损伤蛋白的重折叠或处理,有助于维持蛋白质网络。在多细胞生物中,细胞会持续受到机械力产生的应激的影响。然而,很长一段时间以来,机械应激并没有被认为是一种主要的应激源,它会破坏蛋白质结构并威胁蛋白质组的完整性。识别和描述处理力折叠蛋白的蛋白质折叠和降解系统标志着这方面的一个转折点。显然,机械应激保护在细胞分化、黏附和迁移过程中发挥作用,对于维持骨骼肌肉、心脏和肾脏以及免疫系统等组织的正常功能至关重要。在这里,我们概述了我们在理解机械应激保护方面的最新进展。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8629/8339670/8b56f7c4cb59/EMBR-22-e52507-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8629/8339670/42b94fcc5fb1/EMBR-22-e52507-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8629/8339670/b0dcafd26ad0/EMBR-22-e52507-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8629/8339670/09350c095b10/EMBR-22-e52507-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8629/8339670/cf6a24604082/EMBR-22-e52507-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8629/8339670/8b56f7c4cb59/EMBR-22-e52507-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8629/8339670/42b94fcc5fb1/EMBR-22-e52507-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8629/8339670/b0dcafd26ad0/EMBR-22-e52507-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8629/8339670/09350c095b10/EMBR-22-e52507-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8629/8339670/cf6a24604082/EMBR-22-e52507-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8629/8339670/8b56f7c4cb59/EMBR-22-e52507-g005.jpg

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