title: Redox regulation of mitochondrial ATP synthase.
abstract: Reversible cysteine oxidative post-translational modifications (Ox-PTMs) represent an important mechanism to regulate protein structure and function. In mitochondria, redox reactions can modulate components of the electron transport chain (ETC), the F(1)F(0)-ATP synthase complex, and other matrix proteins/enzymes. Emerging evidence has linked Ox-PTMs to mitochondrial dysfunction and heart failure, highlighting some potential therapeutic avenues. Ox-PTMs can modify a variety of amino acid residues, including cysteine, and have the potential to modulate the function of a large number of proteins. Among this group, there is a selected subset of amino acid residues that can function as redox switches. These unique sites are proposed to monitor the cell's oxidative balance through their response to the various Ox-PTMs. In this review, the role of Ox-PTMs in the regulation of the F(1)F(0)-ATP synthase complex is discussed in the context of heart failure and its possible clinical treatment.
authors: Sheng-Bing Wang is at the Division of Cardiology, Department of Medicine, School of Medicine, Johns Hopkins University, Baltimore, MD 21224, USA.
authors: Sheng-Bing
authors: SB
authors: Wang
authors: Christopher I
authors: CI
authors: Murray
authors: Heaseung S
authors: HS
authors: Chung
authors: Jennifer E
authors: JE
authors: Van Eyk
mesh_terms: D003545:Cysteine / Q000235:genetics* / Q000378:metabolism; D006333:Heart Failure / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008928:Mitochondria / Q000201:enzymology* / Q000235:genetics; D025261:Mitochondrial Proton-Translocating ATPases / Q000235:genetics / Q000378:metabolism*; D010084:Oxidation-Reduction; D018384:Oxidative Stress / Q000235:genetics*; D011499:Protein Processing, Post-Translational / Q000235:genetics*
chemical_list: D025261:Mitochondrial Proton-Translocating ATPases; D003545:Cysteine