Proteome Turnover in the Spotlight: Approaches, Applications, and Perspectives.
Proteome Turnover in the Spotlight: Approaches, Applications, and Perspectives.
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聚光灯下的蛋白质组周转：方法，应用和前景。
DOI：
10.1074/mcp.r120.002190
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发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Jovanovic M
中科院分区：
文献类型：
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作者：
Ross AB;Langer JD;Jovanovic M
在所有细胞中，蛋白质不断合成和降解，以维持蛋白质稳态并响应刺激改变基因表达水平。总的来说，蛋白质合成和降解的过程被称为蛋白质周转。在稳定状态下，蛋白质周转是恒定的，以维持蛋白质稳态，但在动态响应中，蛋白质改变其合成和降解速率，以调节其蛋白质组以适应内部或外部刺激。因此，探索蛋白质周转的动力学和动力学有助于深入了解细胞如何调节生长，分化和应激反应等基本过程。在这里，我们概述了历史和当前的方法来测量蛋白质周转动力学的蛋白质组范围内的稳态和动态系统，重点是代谢示踪使用稳定的同位素标记的氨基酸。我们强调设计蛋白质组周转实验的重要考虑因素，关于蛋白质组周转调节的保守原则的关键生物学发现，以及技术和生物学研究的未来前景。细胞蛋白质处于不断的合成和降解过程中。质谱法能够对蛋白质组转换进行全面的定量分析。几种标记策略提供了直接的蛋白质组周转测量。蛋白质组周转研究已经回答了各种重要的生物学问题。在这篇综述中，我们概述了历史和目前的方法来衡量蛋白质组范围内的稳态和动态系统的蛋白质周转动力学，重点是代谢示踪使用稳定的同位素标记的氨基酸。此外，我们强调设计蛋白质组营业额的实验，关键的生物学研究结果的保守原则的蛋白质组营业额调节，以及未来的前景，为技术和生物学研究的重要考虑因素。
In all cells, proteins are continuously synthesized and degraded to maintain protein homeostasis and modify gene expression levels in response to stimuli. Collectively, the processes of protein synthesis and degradation are referred to as protein turnover. At a steady state, protein turnover is constant to maintain protein homeostasis, but in dynamic responses, proteins change their rates of synthesis and degradation to adjust their proteomes to internal or external stimuli. Thus, probing the kinetics and dynamics of protein turnover lends insight into how cells regulate essential processes such as growth, differentiation, and stress response. Here, we outline historical and current approaches to measuring the kinetics of protein turnover on a proteome-wide scale in both steady-state and dynamic systems, with an emphasis on metabolic tracing using stable isotope–labeled amino acids. We highlight important considerations for designing proteome turnover experiments, key biological findings regarding the conserved principles of proteome turnover regulation, and future perspectives for both technological and biological investigation. Cellular proteins are in constant flux of synthesis and degradation. Mass spectrometry enables comprehensive, quantitative analyses of proteome turnover. Several labeling strategies provide direct proteome turnover measurements. Proteome turnover studies have answered a variety of important biological questions. In this review, we outline historical and current approaches to measure the kinetics of protein turnover on a proteome-wide scale in both steady-state and dynamic systems, with an emphasis on metabolic tracing using stable isotope–labeled amino acids. In addition, we highlight important considerations for designing proteome turnover experiments, key biological findings regarding the conserved principles of proteome turnover regulation, and future perspectives for both technological and biological investigations.