The ClpP protease is found across eukaryotic and prokaryotic organisms. It is well-characterized in bacteria where its function is important in maintaining protein homeostasis. Along with its ATPase partners, it has been shown to play critical roles in the regulation of enzymes involved in important cellular pathways. In eukaryotes, ClpP is found within cellular organelles. Proteomic studies have begun to characterize the role of this protease in the mitochondria through its interactions. Here, we discuss the proteomic techniques used to identify its interactors and present an atlas of mitochondrial ClpP substrates. The ClpP substrate pool is extensive and consists of proteins involved in essential mitochondrial processes such as the Krebs cycle, oxidative phosphorylation, translation, fatty acid metabolism, and amino acid metabolism. Discoveries of these associations have begun to illustrate the functional significance of ClpP in human health and disease.

ClpP 蛋白酶存在于真核生物和原核生物中。它在细菌中具有很好的特征，其功能对于维持蛋白质稳态很重要。与它的 ATPase 合作伙伴一起，它已被证明在调节参与重要细胞途径的酶方面发挥关键作用。在真核生物中，ClpP 存在于细胞器中。蛋白质组学研究已经开始通过其相互作用来表征这种蛋白酶在线粒体中的作用。在这里，我们讨论了用于识别其相互作用物并呈现线粒体 ClpP 底物图谱的蛋白质组学技术。ClpP 底物库是广泛的，由参与基本线粒体过程的蛋白质组成，例如克雷布斯循环、氧化磷酸化、翻译、脂肪酸代谢和氨基酸代谢。