Oxidative folding in the mitochondrial intermembrane space: a regulated process important for cell physiology and disease

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Chatzi, Afroditi ; Manganas, Phanee ; Tokatlidis, Kostas (2016)
  • Publisher: Elsevier
  • Journal: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, volume 1,863, issue 6, pages 1,298-1,306 (issn: 0167-4889, eissn: 1878-2434)
  • Related identifiers: pmc: PMC5405047, doi: 10.1016/j.bbamcr.2016.03.023
  • Subject: MPP, Mitochondria processing peptidase | Molecular Biology | Ccs, Copper chaperone for SOD1 | QSOX, Quiescin–sulfhydryl oxidase | CHCH, coiled coil–helix–coiled coil–helix | Thiol-disulfide exchange | GSH, reduced glutathione | GSSG, oxidized glutathione | HPO, hepatopoietin protein | Erv1 | TIM, Translocase of the inner mitochondrial membrane | HSS, Hepatic regenerative stimulation substance | ALR, Augmenter of liver regeneration (also called GFER, HPO, HSS) | MIA, Mitochondria import and assembly | COX, cytochrome C oxidase | SOD, Superoxide dismutase | TOM, Translocase of the outer mitochondrial membrane | Drp, Dynamin related GTPase protein | Review | SAM, sorting and assembly machinery | MISS, Mitochondrial intermembrane space sorting signal | NMR, Nuclear magnetic resonance | CytC, cytochrome C | Ero, Endoplasmic reticulum oxidation gene | CPC, Cysteine–Proline–Cysteine tripeptide | IMS, Intermembrane space | ER, Endoplasmic reticulum | Aim, Altered inheritance of mitochondria | Hot, Helper of Tim | PDI, Protein disulfide isomerase | Mitochondrial intermembrane space | Dsb, Disulfide bond formation genes | MICOS, Mitochondrial contact site and cristae organizing system | GFER, Growth factor, Erv1-like protein | HSP, Heat shock protein | Oxidative protein folding | Mia40 | Cell Biology | Mitochondrial protein import | Erv, Essential for respiration and viability | CIA, cytosolic iron/sulphur cluster assembly | FAD, flavin adenine dinucleotide | ITS, Intermembrane space targeting signal

Mitochondria are fundamental organelles with a complex internal architecture that fulfill important diverse functions including iron–sulfur cluster assembly and cell respiration. Intense work for more than 30 years has identified the key protein import components and the pathways involved in protein targeting and assembly. More recently, oxidative folding has been discovered as one important mechanism for mitochondrial proteostasis whilst several human disorders have been linked to this pathway. We describe the molecular components of this pathway in view of their putative redox regulation and we summarize available evidence on the connections of these pathways to human disorders.
  • References (146)
    146 references, page 1 of 15

    [1] S.E. Horvath, G. Daum, Lipids of mitochondria, Prog. Lipid Res. (2013) 590-614.

    [2] Y. Tamura, H. Sesaki, T. Endo, Phospholipid transport via mitochondria, Traffic 15 (2014) 933-945.

    [3] M.G. Baile, Y.-W. Lu, S.M. Claypool, The topology and regulation of cardiolipin biosynthesis and remodeling in yeast, Chem. Phys. Lipids 179 (2014) 25-31.

    [4] N. Joza, S.A. Susin, E. Daugas, W.L. Stanford, S.K. Cho, C.Y. Li, T. Sasaki, A.J. Elia, H.Y. Cheng, L. Ravagnan, K.F. Ferri, N. Zamzami, A. Wakeham, R. Hakem, H. Yoshida, Y.Y. Kong, T.W. Mak, J.C. Zúñiga-Pflücker, G. Kroemer, J.M. Penninger, Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death, Nature 410 (2001) 549-554.

    [5] R. Lill, Function and biogenesis of iron-sulphur proteins, Nature 460 (2009) 831-838.

    [6] R. Lill, V. Srinivasan, U. Mühlenhoff, The role of mitochondria in cytosolic-nuclear iron-sulfur protein biogenesis and in cellular iron regulation, Curr. Opin. Microbiol. 22 (2014) 111-119.

    [7] H.M. McBride, M. Neuspiel, S. Wasiak, Mitochondria: more than just a powerhouse, Curr. Biol. 16 (2006) R551-R560.

    [8] D. Milenkovic, J. Müller, D. Stojanovski, N. Pfanner, A. Chacinska, Diverse mechanisms and machineries for import of mitochondrial proteins, Biol. Chem. 388 (2007) 891-897.

    [9] A. Chacinska, C.M. Koehler, D. Milenkovic, T. Lithgow, N. Pfanner, Importing mitochondrial proteins: machineries and mechanisms, Cell 138 (2009) 628-644.

    [10] D.P. Sideris, K. Tokatlidis, Oxidative protein folding in the mitochondrial intermembrane space, Antioxid. Redox Signal. 13 (2010) 1189-1204.

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