title: Emerging role of Lon protease as a master regulator of mitochondrial functions.
abstract: Lon protease is a nuclear-encoded, mitochondrial ATP-dependent protease highly conserved throughout the evolution, crucial for the maintenance of mitochondrial homeostasis. Lon acts as a chaperone of misfolded proteins, and is necessary for maintaining mitochondrial DNA. The impairment of these functions has a deep impact on mitochondrial functionality and morphology. An altered expression of Lon leads to a profound reprogramming of cell metabolism, with a switch from respiration to glycolysis, which is often observed in cancer cells. Mutations of Lon, which likely impair its chaperone properties, are at the basis of a genetic inherited disease named of the cerebral, ocular, dental, auricular, skeletal (CODAS) syndrome. This article is part of a Special Issue entitled 'EBEC 2016: 19th European Bioenergetics Conference, Riva del Garda, Italy, July 2-6, 2016', edited by Prof. Paolo Bernardi.
authors.affiliation: Department of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy.
authors.forename: Marcello
authors.initials: M
authors.lastname: Pinti
authors.affiliation: Department of Surgery, Medicine, Dentistry and Morphological Sciences, University of Modena and Reggio Emilia, Modena, Italy.
authors.forename: Lara
authors.initials: L
authors.lastname: Gibellini
authors.affiliation: Department of Surgery, Medicine, Dentistry and Morphological Sciences, University of Modena and Reggio Emilia, Modena, Italy.
authors.forename: Milena
authors.initials: M
authors.lastname: Nasi
authors.affiliation: Department of Surgery, Medicine, Dentistry and Morphological Sciences, University of Modena and Reggio Emilia, Modena, Italy.
authors.forename: Sara
authors.initials: S
authors.lastname: De Biasi
authors.affiliation: Department of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy.
authors.forename: Carlo Augusto
authors.initials: CA
authors.lastname: Bortolotti
authors.affiliation: Department of Diagnostics, Clinical and Public Health Medicine, University of Modena and Reggio Emilia, Modena, Italy.
authors.forename: Anna
authors.initials: A
authors.lastname: Iannone
authors.affiliation: Department of Surgery, Medicine, Dentistry and Morphological Sciences, University of Modena and Reggio Emilia, Modena, Italy. Electronic address: andrea.cossarizza@unimore.it.
authors.forename: Andrea
authors.initials: A
authors.lastname: Cossarizza
mesh_terms: D065150:Cellular Reprogramming; D019465:Craniofacial Abnormalities / Q000201:enzymology / Q000235:genetics* / Q000473:pathology; D004272:DNA, Mitochondrial / Q000235:genetics* / Q000378:metabolism; D005124:Eye Abnormalities / Q000201:enzymology / Q000235:genetics* / Q000473:pathology; D006130:Growth Disorders / Q000201:enzymology / Q000235:genetics* / Q000473:pathology; D006618:Hip Dislocation, Congenital / Q000201:enzymology / Q000235:genetics* / Q000473:pathology; D006706:Homeostasis; D006801:Humans; D008928:Mitochondria / Q000201:enzymology* / Q000473:pathology; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D009154:Mutation; D010009:Osteochondrodysplasias / Q000201:enzymology / Q000235:genetics* / Q000473:pathology; D049070:Protease La / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017510:Protein Folding; D014071:Tooth Abnormalities / Q000201:enzymology / Q000235:genetics* / Q000473:pathology
chemical_list: D004272:DNA, Mitochondrial; D018832:Molecular Chaperones; D049070:Protease La
keywords: CODAS syndrome; Cancer; Chaperone; Lon; Mitochondria; Protease; mtDNA