|
[1] Omura, T. (1998) Mitochondria-targeting sequence, a multi-role sorting sequence recognized at all steps of protein import into mitochondria, J Biochem 123, 1010-1016. [2] Boekema, E. J., and Braun, H. P. (2007) Supramolecular structure of the mitochondrial oxidative phosphorylation system, J Biol Chem 282, 1-4. [3] Li, Y., Park, J. S., Deng, J. H., and Bai, Y. (2006) Cytochrome c oxidase subunit IV is essential for assembly and respiratory function of the enzyme complex, J Bioenerg Biomembr 38, 283-291. [4] Perry, S. W., Norman, J. P., Barbieri, J., Brown, E. B., and Gelbard, H. A. (2011) Mitochondrial membrane potential probes and the proton gradient: a practical usage guide, Biotechniques 50, 98-115. [5] Smeitink, J., van den Heuvel, L., and DiMauro, S. (2001) The genetics and pathology of oxidative phosphorylation, Nat Rev Genet 2, 342-352. [6] Chacinska, A., Koehler, C. M., Milenkovic, D., Lithgow, T., and Pfanner, N. (2009) Importing Mitochondrial Proteins: Machineries and Mechanisms, Cell 138, 628-644. [7] Andrews, B., Carroll, J., Ding, S., Fearnley, I. M., and Walker, J. E. (2013) Assembly factors for the membrane arm of human complex I, Proc Natl Acad Sci U S A 110, 18934-18939. [8] Sazanov, L. A., and Hinchliffe, P. (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus, Science 311, 1430-1436. [9] Mathiesen, C., and Hagerhall, C. (2002) Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters, Biochim Biophys Acta 1556, 121-132. [10] Hinchliffe, P., and Sazanov, L. A. (2005) Organization of iron-sulfur clusters in respiratory complex I, Science 309, 771-774. [11] Hirst, J., Carroll, J., Fearnley, I. M., Shannon, R. J., and Walker, J. E. (2003) The nuclear encoded subunits of complex I from bovine heart mitochondria, Biochim Biophys Acta 1604, 135-150. [12] Ohnishi, T. (1998) Iron-sulfur clusters/semiquinones in complex I, Biochim Biophys Acta 1364, 186-206. [13] Hyslop, S. J., Duncan, A. M., Pitkanen, S., and Robinson, B. H. (1996) Assignment of the PSST subunit gene of human mitochondrial complex I to chromosome 19p13, Genomics 37, 375-380. [14] Lebon, S., Minai, L., Chretien, D., Corcos, J., Serre, V., Kadhom, N., Steffann, J., Pauchard, J. Y., Munnich, A., Bonnefont, J. P., and Rotig, A. (2007) A novel mutation of the NDUFS7 gene leads to activation of a cryptic exon and impaired assembly of mitochondrial complex I in a patient with Leigh syndrome, Mol Genet Metab 92, 104-108. [15] Triepels, R. H., van den Heuvel, L. P., Loeffen, J. L., Buskens, C. A., Smeets, R. J., Rubio Gozalbo, M. E., Budde, S. M., Mariman, E. C., Wijburg, F. A., Barth, P. G., Trijbels, J. M., and Smeitink, J. A. (1999) Leigh syndrome associated with a mutation in the NDUFS7 (PSST) nuclear encoded subunit of complex I, Ann Neurol 45, 787-790. [16] Frykman, S., Teranishi, Y., Hur, J. Y., Sandebring, A., Yamamoto, N. G., Ancarcrona, M., Nishimura, T., Winblad, B., Bogdanovic, N., Schedin-Weiss, S., Kihara, T., and Tjernberg, L. O. (2012) Identification of two novel synaptic gamma-secretase associated proteins that affect amyloid beta-peptide levels without altering Notch processing, Neurochem Int 61, 108-118. [17] Andreazza, A. C., Shao, L., Wang, J., and Young, L. (2010) Mitochondrial complex I activity and oxidative damage to mitochondrial proteins in the prefrontal cortex of patients with bipolar disorder, Archives of General Psychiatry 67, 360-368. [18] Schwartz, D. C., and Hochstrasser, M. (2003) A superfamily of protein tags: ubiquitin, SUMO and related modifiers, Trends in Biochemical Sciences 28, 321-328. [19] Meluh, P. B., and Koshland, D. (1995) Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a centromere protein with homology to the mammalian centromere protein CENP-C, Mol Biol Cell 6, 793-807. [20] Shen, Z., Pardington-Purtymun, P. E., Comeaux, J. C., Moyzis, R. K., and Chen, D. J. (1996) UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins, Genomics 36, 271-279. [21] Okura, T., Gong, L., Kamitani, T., Wada, T., Okura, I., Wei, C. F., Chang, H. M., and Yeh, E. T. (1996) Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin, J Immunol 157, 4277-4281. [22] Mahajan, R., Delphin, C., Guan, T., Gerace, L., and Melchior, F. (1997) A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2, Cell 88, 97-107. [23] Tanaka, K., Nishide, J., Okazaki, K., Kato, H., Niwa, O., Nakagawa, T., Matsuda, H., Kawamukai, M., and Murakami, Y. (1999) Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation, Mol Cell Biol 19, 8660-8672. [24] Bohren, K. M., Nadkarni, V., Song, J. H., Gabbay, K. H., and Owerbach, D. (2004) A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus, J Biol Chem 279, 27233-27238. [25] Melchior, F. (2000) SUMO--nonclassical ubiquitin, Annu Rev Cell Dev Biol 16, 591-626. [26] Klein, U. R., Haindl, M., Nigg, E. A., and Muller, S. (2009) RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin, Mol Biol Cell 20, 410-418. [27] Wang, C. Y., and She, J. X. (2008) SUMO4 and its role in type 1 diabetes pathogenesis, Diabetes Metab Res Rev 24, 93-102. [28] Wang, C.-Y., Yang, P., Li, M., and Gong, F. (2009) Characterization of a negative feedback network between SUMO4 expression and NFκB transcriptional activity, Biochemical and Biophysical Research Communications 381, 477-481. [29] Hickey, C. M., Wilson, N. R., and Hochstrasser, M. (2012) Function and regulation of SUMO proteases, Nat Rev Mol Cell Biol 13, 755-766. [30] Gong, L., Li, B., Millas, S., and Yeh, E. T. (1999) Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex, FEBS Lett 448, 185-189. [31] Bernier-Villamor, V., Sampson, D. A., Matunis, M. J., and Lima, C. D. (2002) Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1, Cell 108, 345-356. [32] Droescher, M., Chaugule, V. K., and Pichler, A. (2013) SUMO rules: regulatory concepts and their implication in neurologic functions, Neuromolecular Med 15, 639-660. [33] Matic, I., Schimmel, J., Hendriks, I. A., van Santen, M. A., van de Rijke, F., van Dam, H., Gnad, F., Mann, M., and Vertegaal, A. C. (2010) Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif, Mol Cell 39, 641-652. [34] Pichler, A., Knipscheer, P., Oberhofer, E., van Dijk, W. J., Korner, R., Olsen, J. V., Jentsch, S., Melchior, F., and Sixma, T. K. (2005) SUMO modification of the ubiquitin-conjugating enzyme E2-25K, Nat Struct Mol Biol 12, 264-269. [35] Hietakangas, V., Anckar, J., Blomster, H. A., Fujimoto, M., Palvimo, J. J., Nakai, A., and Sistonen, L. (2006) PDSM, a motif for phosphorylation-dependent SUMO modification, Proc Natl Acad Sci U S A 103, 45-50. [36] Picard, N., Caron, V., Bilodeau, S., Sanchez, M., Mascle, X., Aubry, M., and Tremblay, A. (2012) Identification of estrogen receptor beta as a SUMO-1 target reveals a novel phosphorylated sumoylation motif and regulation by glycogen synthase kinase 3beta, Mol Cell Biol 32, 2709-2721. [37] Yang, S. H., Galanis, A., Witty, J., and Sharrocks, A. D. (2006) An extended consensus motif enhances the specificity of substrate modification by SUMO, EMBO J 25, 5083-5093. [38] Lamoliatte, F., Bonneil, E., Durette, C., Caron-Lizotte, O., Wildemann, D., Zerweck, J., Wenshuk, H., and Thibault, P. (2013) Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions, Mol Cell Proteomics 12, 2536-2550. [39] Praefcke, G. J. K., Hofmann, K., and Dohmen, R. J. (2012) SUMO playing tag with ubiquitin, Trends in Biochemical Sciences 37, 23-31. [40] Ullmann, R., Chien, C. D., Avantaggiati, M. L., and Muller, S. (2012) An acetylation switch regulates SUMO-dependent protein interaction networks, Mol Cell 46, 759-770. [41] Cubenas-Potts, C., and Matunis, M. J. (2013) SUMO: a multifaceted modifier of chromatin structure and function, Dev Cell 24, 1-12. [42] Flotho, A., and Melchior, F. (2013) Sumoylation: a regulatory protein modification in health and disease, Annu Rev Biochem 82, 357-385. [43] Hudson, J. J. R., Chiang, S.-C., Wells, O. S., Rookyard, C., and El-Khamisy, S. F. (2012) SUMO modification of the neuroprotective protein TDP1 facilitates chromosomal single-strand break repair, Nat Commun 3, 733. [44] Steffan, J. S., Agrawal, N., Pallos, J., Rockabrand, E., Trotman, L. C., Slepko, N., Illes, K., Lukacsovich, T., Zhu, Y. Z., Cattaneo, E., Pandolfi, P. P., Thompson, L. M., and Marsh, J. L. (2004) SUMO modification of Huntingtin and Huntington's disease pathology, Science 304, 100-104. [45] Sapir, A., Tsur, A., Koorman, T., Ching, K., Mishra, P., Bardenheier, A., Podolsky, L., Bening-Abu-Shach, U., Boxem, M., Chou, T. F., Broday, L., and Sternberg, P. W. (2014) Controlled sumoylation of the mevalonate pathway enzyme HMGS-1 regulates metabolism during aging, Proc Natl Acad Sci U S A 111, E3880-3889. [46] Zhang, J., Yuan, C., Wu, J., Elsayed, Z., and Fu, Z. (2015) Polo-like kinase 1-mediated phosphorylation of Forkhead box protein M1b antagonizes its SUMOylation and facilitates its mitotic function, J Biol Chem 290, 3708-3719. [47] Santiago, A., Li, D., Zhao, L. Y., Godsey, A., and Liao, D. (2013) p53 SUMOylation promotes its nuclear export by facilitating its release from the nuclear export receptor CRM1, Mol Biol Cell 24, 2739-2752. [48] Chen, L., Ma, Y., Qian, L., and Wang, J. (2013) Sumoylation regulates nuclear localization and function of zinc finger transcription factor ZIC3, Biochim Biophys Acta 1833, 2725-2733. [49] Saitoh, H., and Hinchey, J. (2000) Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3, J Biol Chem 275, 6252-6258. [50] Tempe, D., Piechaczyk, M., and Bossis, G. (2008) SUMO under stress, Biochem Soc Trans 36, 874-878. [51] Bossis, G., and Melchior, F. (2006) Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes, Mol Cell 21, 349-357. [52] Xu, Z., Lam, L. S., Lam, L. H., Chau, S. F., Ng, T. B., and Au, S. W. (2008) Molecular basis of the redox regulation of SUMO proteases: a protective mechanism of intermolecular disulfide linkage against irreversible sulfhydryl oxidation, FASEB J 22, 127-137. [53] Ke, Q., and Costa, M. (2006) Hypoxia-inducible factor-1 (HIF-1), Mol Pharmacol 70, 1469-1480. [54] Comerford, K. M., Leonard, M. O., Karhausen, J., Carey, R., Colgan, S. P., and Taylor, C. T. (2003) Small ubiquitin-related modifier-1 modification mediates resolution of CREB-dependent responses to hypoxia, Proc Natl Acad Sci U S A 100, 986-991. [55] Wang, J., Wang, Y., and Lu, L. (2012) De-SUMOylation of CCCTC binding factor (CTCF) in hypoxic stress-induced human corneal epithelial cells, J Biol Chem 287, 12469-12479. [56] Fariss, M. W., Chan, C. B., Patel, M., Van Houten, B., and Orrenius, S. (2005) Role of mitochondria in toxic oxidative stress, Mol Interv 5, 94-111. [57] Grattagliano, I., Vendemiale, G., Caraceni, P., Domenicali, M., Nardo, B., Cavallari, A., Trevisani, F., Bernardi, M., and Altomare, E. (2000) Starvation impairs antioxidant defense in fatty livers of rats fed a choline-deficient diet, J Nutr 130, 2131-2136. [58] Prem, P., Parihar, M. S., Malini, L., and Pradeep, K. G. (1998) Starvation induced hypothyroidism involves perturbations in thyroid superoxide-SOD system in pigeons, Biochem Mol Biol Int 45, 73-83. [59] Pirkmajer, S., and Chibalin, A. V. (2011) Serum starvation: caveat emptor, Am J Physiol Cell Physiol 301, C272-279. [60] Guo, D., Han, J., Adam, B. L., Colburn, N. H., Wang, M. H., Dong, Z., Eizirik, D. L., She, J. X., and Wang, C. Y. (2005) Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress, Biochem Biophys Res Commun 337, 1308-1318. [61] Bassi, C., Ho, J., Srikumar, T., Dowling, R. J., Gorrini, C., Miller, S. J., Mak, T. W., Neel, B. G., Raught, B., and Stambolic, V. (2013) Nuclear PTEN controls DNA repair and sensitivity to genotoxic stress, Science 341, 395-399. [62] van der Bliek, A. M. (2000) A Mitochondrial Division Apparatus Takes Shape, The Journal of Cell Biology 151, f1-f4. [63] Harder, Z., Zunino, R., and McBride, H. (2004) Sumo1 conjugates mitochondrial substrates and participates in mitochondrial fission, Curr Biol 14, 340-345. [64] Wasiak, S., Zunino, R., and McBride, H. M. (2007) Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death, J Cell Biol 177, 439-450. [65] Huang, Y., Du, K. M., Xue, Z. H., Yan, H., Li, D., Liu, W., Chen, Z., Zhao, Q., Tong, J. H., Zhu, Y. S., and Chen, G. Q. (2003) Cobalt chloride and low oxygen tension trigger differentiation of acute myeloid leukemic cells: possible mediation of hypoxia-inducible factor-1[alpha], Leukemia 17, 2065-2073. [66] Asikainen, T. M., Schneider, B. K., Waleh, N. S., Clyman, R. I., Ho, W. B., Flippin, L. A., Gunzler, V., and White, C. W. (2005) Activation of hypoxia-inducible factors in hyperoxia through prolyl 4-hydroxylase blockade in cells and explants of primate lung, Proc Natl Acad Sci U S A 102, 10212-10217. [67] Jaakkola, P., Mole, D. R., Tian, Y. M., Wilson, M. I., Gielbert, J., Gaskell, S. J., von Kriegsheim, A., Hebestreit, H. F., Mukherji, M., Schofield, C. J., Maxwell, P. H., Pugh, C. W., and Ratcliffe, P. J. (2001) Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation, Science 292, 468-472. [68] Siddiq, A., Aminova, L. R., Troy, C. M., Suh, K., Messer, Z., Semenza, G. L., and Ratan, R. R. (2009) Selective inhibition of hypoxia-inducible factor prolyl-hydroxylase 1 mediates neuroprotection against normoxic oxidative death via HIF and CREB independent pathways, The Journal of Neuroscience 29, 8828-8838. [69] Cho, E. A., Song, H. K., Lee, S. H., Chung, B. H., Lim, H. M., and Lee, M. K. (2013) Differential in vitro and cellular effects of iron chelators for hypoxia inducible factor hydroxylases, J Cell Biochem 114, 864-873. [70] Hirsila, M., Koivunen, P., Xu, L., Seeley, T., Kivirikko, K. I., and Myllyharju, J. (2005) Effect of desferrioxamine and metals on the hydroxylases in the oxygen sensing pathway, FASEB J 19, 1308-1310. [71] Rambold, A. S., Kostelecky, B., Elia, N., and Lippincott-Schwartz, J. (2011) Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation, Proceedings of the National Academy of Sciences 108, 10190-10195. [72] Böttger, S., Jerszyk, E., Low, B., and Walker, C. (2008) Genotoxic stress–induced expression of p53 and apoptosis in leukemic clam hemocytes with cytoplasmically sequestered p53, Cancer research 68, 777-782. [73] Elmore, S. (2007) Apoptosis: a review of programmed cell death, Toxicol Pathol 35, 495-516. [74] Jamshidiha, M., Habibollahi, P., Ostad, S., and Ghahremani, M. (2010) Primary WWOX phosphorylation and JNK activation during etoposide induces cytotoxicity in HEK293 cells, Daru: journal of Faculty of Pharmacy, Tehran University of Medical Sciences 18, 141. [75] Yuan, Y., Hilliard, G., Ferguson, T., and Millhorn, D. E. (2003) Cobalt inhibits the interaction between hypoxia-inducible factor-α and von Hippel-Lindau protein by direct binding to hypoxia-inducible factor-α, Journal of Biological Chemistry 278, 15911-15916. [76] Triantafyllou, A., Liakos, P., Tsakalof, A., Georgatsou, E., Simos, G., and Bonanou, S. (2006) Cobalt induces hypoxia-inducible factor-1alpha (HIF-1alpha) in HeLa cells by an iron-independent, but ROS-, PI-3K- and MAPK-dependent mechanism, Free Radic Res 40, 847-856. [77] Zhou, J., Schmid, T., Frank, R., and Brüne, B. (2004) PI3K/Akt is required for heat shock proteins to protect hypoxia-inducible factor 1α from pVHL-independent degradation, Journal of Biological Chemistry 279, 13506-13513.
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