Metalloproteases of the Inner Mitochondrial Membrane

Roman M. Levytskyy, Iryna Bohovych, Oleh Khalimonchuk

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

Abstract

The inner mitochondrial membrane (IM) is among the most protein-rich cellular compartments. The metastable IM subproteome where the concentration of proteins is approaching oversaturation creates a challenging protein folding environment with a high probability of protein malfunction or aggregation. Failure to maintain protein homeostasis in such a setting can impair the functional integrity of the mitochondria and drive clinical manifestations. The IM is equipped with a series of highly conserved, proteolytic complexes dedicated to the maintenance of normal protein homeostasis within this mitochondrial subcompartment. Particularly important is a group of membrane-anchored metallopeptidases commonly known as m-AAA and i-AAA proteases, and the ATP-independent Oma1 protease. Herein, we will summarize the current biochemical knowledge of these proteolytic machines and discuss recent advances in our understanding of mechanistic aspects of their functioning.

Original languageEnglish (US)
Pages (from-to)4737-4746
Number of pages10
JournalBiochemistry
Volume56
Issue number36
DOIs
StatePublished - Sep 12 2017

ASJC Scopus subject areas

  • Biochemistry

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