Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12857/115517
Title: The mitochondrial permeability transition pore in AD 2016: An update
Authors: Biasutto, Lucia 
Azzolini, Michele
Szabò, Ildikò
Zoratti, Mario 
Keywords: Cyclophilin D;F(O)F(1) ATP synthase;Mitochondrial permeability transition pore (mPTP);Spastic paraplegia 7 (SPG7)
Keywords Plus: ISCHEMIA-REPERFUSION INJURY;ADENINE-NUCLEOTIDE TRANSLOCASE;M-AAA PROTEASE;CONGENITAL MUSCULAR-DYSTROPHY;RESPIRATORY-CHAIN COMPLEXES;CYCLOPHILIN-D PROTECTS;ADP/ATP CARRIER PROTEIN;DEPENDENT ANION CHANNEL;RAT-LIVER MITOCHONDRIA;F1FO ATP SYNTHASE
Mesh headings: Mitochondrial Membrane Transport Proteins
Secondary Mesh headings: ATPases Associated with Diverse Cellular Activities;Adenosine Triphosphate;Animals;Cyclophilin D;Cyclophilins;Dimerization;Humans;Metalloendopeptidases;Neoplasm Proteins;Neoplasms;Nerve Tissue Proteins;Neurodegenerative Diseases;Proton-Translocating ATPases;Spastic Paraplegia, Hereditary
Issue Date: 2016
Publisher: ELSEVIER SCIENCE BV
Journal: Biochimica et biophysica acta 
Abstract: 
Over the past 30years the mitochondrial permeability transition - the permeabilization of the inner mitochondrial membrane due to the opening of a wide pore - has progressed from being considered a curious artifact induced in isolated mitochondria by Ca(2+) and phosphate to a key cell-death-inducing process in several major pathologies. Its relevance is by now universally acknowledged and a pharmacology targeting the phenomenon is being developed. The molecular nature of the pore remains to this day uncertain, but progress has recently been made with the identification of the FOF1 ATP synthase as the probable proteic substrate. Researchers sharing this conviction are however divided into two camps: these believing that only the ATP synthase dimers or oligomers can form the pore, presumably in the contact region between monomers, and those who consider that the ring-forming c subunits in the FO sector actually constitute the walls of the pore. The latest development is the emergence of a new candidate: Spastic Paraplegia 7 (SPG7), a mitochondrial AAA-type membrane protease which forms a 6-stave barrel. This review summarizes recent developments of research on the pathophysiological relevance and on the molecular nature of the mitochondrial permeability transition pore. This article is part of a Special Issue entitled: Mitochondrial Channels edited by Pierre Sonveaux, Pierre Maechler and Jean-Claude Martinou.
URI: http://hdl.handle.net/20.500.12857/115517
ISSN: 0006-3002
DOI: 10.1016/j.bbamcr.2016.02.012
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