Redox Regulation of the Conserved Mitochondrial Protease Oma1

Bohovych, Iryna; Dietz, Jonathan V.; Swenson, Samantha; Zahayko, Nataliya; Khalimonchuk, Oleh

doi:10.1016/j.freeradbiomed.2017.10.215

Cited by 1 publication

(1 citation statement)

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“…Data indicate that only thiol-containing reductants decrease the proteolytic activity of Oma1. Moreover, the proteases lacking these cysteine residues are less sensitive to reduction [100]. A similar mechanism was found in serine enterobacterial Lon protease, which has been proposed to function as a switch to optimize Lon's proteolytic activity depending on the redox environment [101].…”

Section: Initiation Of Rcdmentioning

confidence: 72%

Redox-Mediated Post-Translational Modifications of Proteolytic Enzymes and Their Role in Protease Functioning

Petushkova

Zamyatnin

2020

Biomolecules

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Proteolytic enzymes play a crucial role in metabolic processes, providing the cell with amino acids through the hydrolysis of multiple endogenous and exogenous proteins. In addition to this function, proteases are involved in numerous protein cascades to maintain cellular and extracellular homeostasis. The redox regulation of proteolysis provides a flexible dose-dependent mechanism for proteolytic activity control. The excessive reactive oxygen species (ROS) and reactive nitrogen species (RNS) in living organisms indicate pathological conditions, so redox-sensitive proteases can swiftly induce pro-survival responses or regulated cell death (RCD). At the same time, severe protein oxidation can lead to the dysregulation of proteolysis, which induces either protein aggregation or superfluous protein hydrolysis. Therefore, oxidative stress contributes to the onset of age-related dysfunction. In the present review, we consider the post-translational modifications (PTMs) of proteolytic enzymes and their impact on homeostasis.

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Section: Initiation Of Rcdmentioning

confidence: 72%