title: Mitochondrial dismissal in mammals, from protein degradation to mitophagy.
abstract: Mitochondria are double-membraned highly dynamic organelles; the shape, location and function of which are determined by a constant balance between opposing fusion and fission events. A fine modulation of mitochondrial structure is crucial for their correct functionality and for many physiological cell processes, the status of these organelles, being thus a key aspect in a cell's fate. Indeed, the homeostasis of mitochondria needs to be highly regulated for the above mentioned reasons, and since a) they are the major source of energy; b) they participate in various signaling pathways; albeit at the same time c) they are also the major source of reactive oxygen species (ROS, the main damaging detrimental players for all cell components). Elaborate mechanisms of mitochondrial quality control have evolved for maintaining a functional mitochondrial network and avoiding cell damage. The first mechanism is the removal of damaged mitochondrial proteins within the organelle via chaperones and protease; the second is the cytosolic ubiquitin-proteasome system (UPS), able to eliminate proteins embedded in the outer mitochondrial membrane; the third is the removal of the entire mitochondria through mitophagy, in the case of extensive organelle damage and dysfunction. In this review, we provide an overview of these mitochondria stability and quality control mechanisms, highlighting mitophagy, and emphasizing the central role of mitochondrial dynamics in this context. This article is part of a Special Issue entitled: Dynamic and ultrastructure of bioenergetic membranes and their components.
authors.affiliation: IRCCS Fondazione Santa Lucia, 00143 Rome, Italy. Electronic address: s.campello@hsantalucia.it.
authors.forename: Silvia
authors.initials: S
authors.lastname: Campello
authors.affiliation: IRCCS Fondazione Santa Lucia, 00143 Rome, Italy; Department of Biology, University of Rome Tor Vergata, 00133 Rome, Italy.
authors.forename: Flavie
authors.initials: F
authors.lastname: Strappazzon
authors.affiliation: IRCCS Fondazione Santa Lucia, 00143 Rome, Italy; Department of Biology, University of Rome Tor Vergata, 00133 Rome, Italy; Unit of Cell Stress and Survival, Danish Cancer Society Research Center, Strandboulevarden 49, 2100 Copenhagen Ø, Denmark. Electronic address: francesco.cecconi@uniroma2.it.
authors.forename: Francesco
authors.initials: F
authors.lastname: Cecconi
mesh_terms: D000818:Animals; D001343:Autophagy; D006801:Humans; D063154:Mitochondrial Dynamics / Q000502:physiology*; D024101:Mitochondrial Proteins / Q000378:metabolism*; D063306:Mitophagy / Q000502:physiology*; D008954:Models, Biological; D059748:Proteolysis; D017382:Reactive Oxygen Species / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D024101:Mitochondrial Proteins; D017382:Reactive Oxygen Species
keywords: Autophagy; Mitochondria Quality Control; Mitochondria fusion/fission; Mitochondrion; Neurodegeneration; Ubiquitylation