Transition metals activate TFEB in overexpressing cells

Biochemical Journal

Volumn 470, Issue 1, 2015, Pages 65-76

  Peña, Karina A ^a   Kiselyov, Kirill ^a  

^a UNIVERSITY OF PITTSBURGH   (United States)

Author keywords

Copper; Lysosomes; Transcription factor; Transcription factor EB (TFEB); Transition metals

Indexed keywords

CATHEPSIN B; CATHEPSIN D; COPPER CHLORIDE; COPPER ZINC SUPEROXIDE DISMUTASE; FERROUS CHLORIDE; GLUTATHIONE; HEME OXYGENASE 1; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MESSENGER RNA; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR EB; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG; BASIC HELIX LOOP HELIX LEUCINE ZIPPER TRANSCRIPTION FACTOR; CHLORIDE; COPPER; CUPRIC CHLORIDE; FERRIC CHLORIDE; FERRIC ION; TFEB PROTEIN, HUMAN; TRANSITION ELEMENT;

ANTIOXIDANT RESPONSIVE ELEMENT; ARTICLE; AUTOPHAGY; CELL COUNT; CELL DAMAGE; CELL FRACTIONATION; CELL MEMBRANE DEPOLARIZATION; CELL PROTECTION; CELL STRESS; CONCENTRATION (PARAMETERS); CONSENSUS SEQUENCE; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVATION; ENZYME REPRESSION; EXOCYTOSIS; GENE OVEREXPRESSION; GENE TRANSLOCATION; GENETIC TRANSFECTION; HOMEOSTASIS; HUMAN; HUMAN CELL; HYPERPOLARIZATION; LYSOSOME; MITOCHONDRIAL MEMBRANE POTENTIAL; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DEPHOSPHORYLATION; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; UPREGULATION; BIOSYNTHESIS; DRUG EFFECTS; GENE EXPRESSION REGULATION; HEK293 CELL LINE; HELA CELL LINE; PHYSIOLOGY;

BASIC HELIX-LOOP-HELIX LEUCINE ZIPPER TRANSCRIPTION FACTORS; CHLORIDES; COPPER; FERRIC COMPOUNDS; GENE EXPRESSION REGULATION; HEK293 CELLS; HELA CELLS; HUMANS; OXIDATIVE STRESS; TRANSITION ELEMENTS;

EID: 84938784867     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20140645     Document Type: Article

References (86)

1. Bleackley, M.R. and Macgillivray, R.T. (2011) Transition metal homeostasis: from yeast to human disease. Biometals 24, 785-809 CrossRef PubMed
2. Pankit, A.N. and Bhave, S.A. (2002) Copper metabolic defects and liver disease: environmental aspects. J. Gastroenterol. Hepatol 17 Suppl 3, S403-S407 CrossRef PubMed
3. Aston, N.S., Watt, N., Morton, I.E., Tanner, M.S. and Evans, G.S. (2000) Copper toxicity affects proliferation and viability of human hepatoma cells (HepG2 line). Hum. Exp. Toxicol. 19, 367-376 CrossRef PubMed
4. Hayashi, H., Yano, M., Fujita, Y. and Wakusawa, S. (2006) Compound overload of copper and iron in patients with Wilson's disease. Med. Mol. Morphol 39, 121-126 CrossRef PubMed
5. Llanos, R.M. and Mercer, J.F. (2002) The molecular basis of copper homeostasis copper-related disorders. DNA Cell Biol 21, 259-270 CrossRef PubMed
6. Schrag, M., Mueller, C., Oyoyo, U., Smith, M.A. and Kirsch, W.M. (2011) Iron, zinc and copper in the Alzheimer's disease brain: a quantitative meta-analysis. Some insight on the influence of citation bias on scientific opinion. Prog. Neurobiol. 94, 296-306 CrossRef PubMed
7. Shcherbatykh, I. and Carpenter, D.O. (2007) The role of metals in the etiology of Alzheimer's disease. J. Alzheimers Dis. 11, 191-205 PubMed
8. Tougu, V., Tiiman, A. and Palumaa, P. (2011) Interactions of Zn(II) and Cu(II) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity. Metallomics 3, 250-261 CrossRef PubMed
9. Ward, R.J., Dexter, D.T. and Crichton, R.R. (2012) Chelating agents for neurodegenerative diseases. Curr. Med. Chem 19, 2760-2772 CrossRef PubMed
10. Dexter, D.T., Carayon, A., Javoy, A.F., Agid, Y., Wells, F.R., Daniel, S.E., Lees, A.J., Jenner, P. and Marsden, C.D. (1991) Alterations in the levels of iron, ferritin and other trace metals in Parkinson's disease and other neurodegenerative diseases affecting the basal ganglia. Brain 114, 1953-1975 CrossRef PubMed
11. Dexter, D.T., Sian, J., Rose, S., Hindmarsh, J.G., Mann, V.M., Cooper, J.M., Wells, F.R., Daniel, S.E., Lees, A.J., Schapira, A.H. et al. (1994) Indices of oxidative stress and mitochondrial function in individuals with incidental Lewy body disease. Ann. Neurol. 35, 38-44 CrossRef PubMed
12. Mendez-Alvarez, E., Soto-Otero, R., Hermida-Ameijeiras, A., Lopez-Real, A.M. and Labandeira-Garcia, J.L. (2002) Effects of aluminum and zinc on the oxidative stress caused by 6-hydroxydopamine autoxidation: relevance for the pathogenesis of Parkinson's disease. Biochim. Biophys. Acta 155-168 PubMed
13. Riederer, P., Sofic, E., Rausch, W.D., Schmidt, B., Reynolds, G.P., Jellinger, K. and Youdim, M.B. (1989) Transition metals, ferritin, glutathione, and ascorbic acid in parkinsonian brains. J. Neurochem. 52, 515-520 CrossRef PubMed
14. Barnham, K.J., Masters, C.L. and Bush, A.I. (2004) Neurodegenerative diseases and oxidative stress. Nat. Rev. Drug Discov. 3, 205-214 CrossRef PubMed
15. Halliwell, B. and Gutteridge, J.M.C. (1984) Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 219, 1-14 PubMed
16. Hegde, M.L., Hegde, P.M., Rao, K.S. and Mitra, S. (2011) Oxidative genome damage and its repair in neurodegenerative diseases: function of transition metals as a double-edged sword. J. Alzheimers Dis. 24 Suppl 2, 183-198 PubMed
17. Hill, G.M. and Link, J.E. (2009) Transporters in the absorption and utilization of zinc and copper. J. Anim. Sci. 87, E85-E89 CrossRef PubMed
18. Morgan, E.H. and Oates, P.S. (2002) Mechanisms and regulation of intestinal iron absorption. Blood Cells Mol. Dis. 29, 384-399 CrossRef PubMed
19. Bouron, A. and Oberwinkler, J. (2014) Contribution of calcium-conducting channels to the transport of zinc ions. Pflugers Arch 466, 381-387 CrossRef PubMed
20. Kukic, I., Kelleher, S.L. and Kiselyov, K. (2014) Zn2+ efflux through lysosomal exocytosis prevents Zn2+-induced toxicity. J. Cell Sci. 127, 3094-3103 CrossRef PubMed
21. Kukic, I., Lee, J.K., Coblentz, J., Kelleher, S.L. and Kiselyov, K. (2013) Zinc-dependent lysosomal enlargement in TRPML1-deficient cells involves MTF-1 transcription factor and ZnT4 (Slc30a4) transporter. Biochem. J. 451, 155-163 CrossRef PubMed
22. Lopez, V. and Kelleher, S.L. (2009) Zinc transporter-2 (ZnT2) variants are localized to distinct subcellular compartments and functionally transport zinc. Biochem. J. 422, 43-52 CrossRef PubMed
23. Lopez, V., Foolad, F. and Kelleher, S.L. (2011) ZnT2-overexpression represses the cytotoxic effects of zinc hyper-accumulation in malignant metallothionein-null T47D breast tumor cells. Cancer Lett 304, 41-51 CrossRef PubMed
24. Seo, Y.A. and Kelleher, S.L. (2010) Functional analysis of two single nucleotide polymorphisms in SLC30A2 (ZnT2): implications for mammary gland function and breast disease in women. Physiol. Genomics 42A, 219-227 CrossRef PubMed
25. Harada, M., Kawaguchi, T., Kumemura, H., Terada, K., Ninomiya, H., Taniguchi, E., Hanada, S., Baba, S., Maeyama, M., Koga, H. et al. (2005) The Wilson disease protein ATP7B resides in the late endosomes with Rab7 and the Niemann-Pick C1 protein. Am. J. Pathol. 166, 499-510 CrossRef PubMed
26. Chapel, A., Kieffer-Jaquinod, S., Sagne, C., Verdon, Q., Ivaldi, C., Mellal, M., Thirion, J., Jadot, M., Bruley, C., Garin, J. et al. (2013) An extended proteome map of the lysosomal membrane reveals novel potential transporters. Mol. Cell. Proteomics 12, 1572-1588 CrossRef PubMed
27. Polishchuk, E.V., Concilli, M., Iacobacci, S., Chesi, G., Pastore, N., Piccolo, P., Paladino, S., Baldantoni, D., van, I.S.C., Chan, J. et al. (2014) Wilson disease protein ATP7B utilizes lysosomal exocytosis to maintain copper homeostasis. Dev. Cell 29, 686-700 CrossRef PubMed
28. Pena, K., Coblenz, J. and Kiselyov, K. (2015) Brief exposure to copper activates lysosomal exocytosis. Cell Calcium 57, 257-262 CrossRef PubMed
29. Valerio, L.G. (2007) Mammalian iron metabolism. Toxicol. Mech. Methods 17, 497-517 CrossRef PubMed
30. Coblentz, J., St Croix, C. and Kiselyov, K. (2014) Loss of TRPML1 promotes production of reactive oxygen species: is oxidative damage a factor in mucolipidosis type IV? Biochem. J. 457, 361-368 CrossRef PubMed
31. Eichelsdoerfer, J.L., Evans, J.A., Slaugenhaupt, S.A. and Cuajungco, M.P. (2010) Zinc dyshomeostasis is linked with the loss of mucolipidosis IV-associated TRPML1 ion channel. J. Biol. Chem. 285, 34304-34308 CrossRef PubMed
32. Dong, X., Cheng, X., Mills, E., Delling, M., Wang, F., Kurz, T. and Xu, H. (2008) The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel. Nature 455, 992-996 CrossRef PubMed
33. Sardiello, M., Palmieri, M., di Ronza, A., Medina, D.L., Valenza, M., Gennarino, V.A., Di Malta, C., Donaudy, F., Embrione, V., Polishchuk, R.S. et al. (2009) A gene network regulating lysosomal biogenesis and function. Science 325, 473-477 PubMed
34. Settembre, C., Di Malta, C., Polito, V.A., Garcia Arencibia, M., Vetrini, F., Erdin, S., Erdin, S.U., Huynh, T., Medina, D., Colella, P. et al. (2011) TFEB links autophagy to lysosomal biogenesis. Science 332, 1429-1433 CrossRef PubMed
35. Martina, J.A., Diab, H.I., Lishu, L., Jeong, A.L., Patange, S., Raben, N. and Puertollano, R. (2014) The nutrient-responsive transcription factor TFE3 promotes autophagy, lysosomal biogenesis, and clearance of cellular debris. Sci. Signal. 7, ra9CrossRef PubMed
36. Palmieri, M., Impey, S., Kang, H., di Ronza, A., Pelz, C., Sardiello, M. and Ballabio, A. (2011) Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways. Hum. Mol. Genet. 20, 3852-3866 CrossRef PubMed
37. Medina, D.L., Fraldi, A., Bouche, V., Annunziata, F., Mansueto, G., Spampanato, C., Puri, C., Pignata, A., Martina, J.A., Sardiello, M. et al. (2011) Transcriptional activation of lysosomal exocytosis promotes cellular clearance. Dev. Cell. 21, 421-430 CrossRef PubMed
38. Martina, J.A., Chen, Y., Gucek, M. and Puertollano, R. (2012) MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB. Autophagy 8, 903-914 CrossRef PubMed
39. Roczniak-Ferguson, A., Petit, C.S., Froehlich, F., Qian, S., Ky, J., Angarola, B., Walther, T.C. and Ferguson, S.M. (2012) The transcription factor TFEB links mTORC1 signaling to transcriptional control of lysosome homeostasis. Sci. Signal. 5, ra42CrossRef PubMed
40. Settembre, C., Zoncu, R., Medina, D.L., Vetrini, F., Erdin, S., Huynh, T., Ferron, M., Karsenty, G., Vellard, M.C., Facchinetti, V. et al. (2012) A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB. EMBO J 31, 1095-1108 CrossRef PubMed
41. La Spada, A.R. (2012) PPARGC1A/PGC-1alpha, TFEB and enhanced proteostasis in Huntington disease: Defining regulatory linkages between energy production and protein-organelle quality control. Autophagy 8, 1845-1847 CrossRef PubMed
42. Decressac, M., Mattsson, B., Weikop, P., Lundblad, M., Jakobsson, J. and Bjorklund, A. (2013) TFEB-mediated autophagy rescues midbrain dopamine neurons from alpha-synuclein toxicity. Proc. Natl. Acad. Sci. U.S.A. 110, E1817-E1826 CrossRef PubMed
43. Pastore, N., Blomenkamp, K., Annunziata, F., Piccolo, P., Mithbaokar, P., Maria Sepe, R., Vetrini, F., Palmer, D., Ng, P., Polishchuk, E. et al. (2013) Gene transfer of master autophagy regulator TFEB results in clearance of toxic protein and correction of hepatic disease in alpha-1-anti-trypsin deficiency. EMBO Mol. Med. 5, 397-412 CrossRef PubMed
44. Zhitomirsky, B. and Assaraf, Y.G. (2015) Lysosomal sequestration of hydrophobic weak base chemotherapeutics triggers lysosomal biogenesis and lysosome-dependent cancer multidrug resistance. Oncotarget 6, 1143-1156 PubMed
45. Pourahmad, J., Ross, S. and O'Brien, P.J. (2001) Lysosomal involvement in hepatocyte cytotoxicity induced by Cu(2+) but not Cd(2+). Free Radic. Biol. Med. 30, 89-97 CrossRef PubMed
46. Singh, R.P., Kumar, S., Nada, R. and Prasad, R. (2006) Evaluation of copper toxicity in isolated human peripheral blood mononuclear cells and it's attenuation by zinc: ex vivo. Mol. Cell Biochem 282, 13-21 CrossRef PubMed
47. Martina, J.A., Diab, H.I., Li, H. and Puertollano, R. (2014) Novel roles for the MiTF/TFE family of transcription factors in organelle biogenesis, nutrient sensing, and energy homeostasis. Cell. Mol. Life Sci. 71, 2483-2497 CrossRef PubMed
48. Brunk, U.T., Jones, C.B. and Sohal, R.S. (1992) A novel hypothesis of lipofuscinogenesis and cellular aging based on interactions between oxidative stress and autophagocytosis. Mutat. Res. 275, 395-403 CrossRef PubMed
49. Colletti, G.A., Miedel, M.T., Quinn, J., Andharia, N., Weisz, O.A. and Kiselyov, K. (2012) Loss of lysosomal ion channel transient receptor potential channel mucolipin-1 (TRPML1) leads to cathepsin B-dependent apoptosis. J. Biol. Chem. 287, 8082-8091 CrossRef PubMed
50. Dusek, P., Jankovic, J. and Le, W. (2012) Iron dysregulation in movement disorders. Neurobiol. Dis. 46, 1-18CrossRef PubMed
51. Kurz, T., Terman, A., Gustafsson, B. and Brunk, U.T. (2008) Lysosomes in iron metabolism, ageing and apoptosis. Histochem. Cell. Biol. 129, 389-406 CrossRef PubMed
52. Dong, X.P., Cheng, X., Mills, E., Delling, M., Wang, F., Kurz, T. and Xu, H. (2008) The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel. Nature 455, 992-996 CrossRef PubMed
53. Roberts, B.R., Ryan, T.M., Bush, A.I., Masters, C.L. and Duce, J.A. (2012) The role of metallobiology and amyloid-beta peptides in Alzheimer's disease. J. Neurochem 120 Suppl 1, 149-166 CrossRef PubMed
54. Shuttleworth, C.W. and Weiss, J.H. (2011) Zinc: new clues to diverse roles in brain ischemia. Trends Pharmacol. Sci. 32, 480-486 CrossRef PubMed
55. Sensi, S.L., Paoletti, P., Koh, J.Y., Aizenman, E., Bush, A.I. and Hershfinkel, M. (2011) The neurophysiology and pathology of brain zinc. J. Neurosci. 31, 16076-16085 CrossRef PubMed
56. Galasso, S.L. and Dyck, R.H. (2007) The role of zinc in cerebral ischemia. Mol. Med. 13, 380-387 CrossRef PubMed
57. Sheline, C.T., Zhu, J., Zhang, W., Shi, C. and Cai, A.L. (2013) Mitochondrial inhibitor models of Huntington's disease and Parkinson's disease induce zinc accumulation and are attenuated by inhibition of zinc neurotoxicity in vitro or in vivo. Neurodegener. Dis 11, 49-58 CrossRef PubMed
58. Brewer, G.J. (2010) Risks of copper and iron toxicity during aging in humans. Chem. Res. Toxicol. 23, 319-326 CrossRef PubMed
59. Jansen, J., Karges, W. and Rink, L. (2009) Zinc and diabetes-clinical links and molecular mechanisms. J. Nutr. Biochem. 20, 399-417 CrossRef PubMed
60. Hordyjewska, A., Popiolek, L. and Kocot, J. (2014) The many "faces" of copper in medicine and treatment. Biometals 27, 611-621 CrossRef PubMed
61. Wijmenga, C. and Klomp, L.W. (2004) Molecular regulation of copper excretion in the liver. Proc. Nutr. Soc. 63, 31-39 CrossRef PubMed
62. Festa, R.A. and Thiele, D.J. (2011) Copper: an essential metal in biology. Curr. Biol. 21, R877-883 CrossRef PubMed
63. Graper, M.L., Huster, D., Kaler, S.G., Lutsenko, S., Schilsky, M.L. and Thiele, D.J. (2014) Introduction to human disorders of copper metabolism. Ann. N.Y. Acad. Sci. 1314, v-vi CrossRef PubMed
64. Hare, D., Ayton, S., Bush, A. and Lei, P. (2013) A delicate balance: Iron metabolism and diseases of the brain. Front. Aging Neurosci. 5, 34 CrossRef PubMed
65. Zheng, Z., Lee, J.E. and Yenari, M.A. (2003) Stroke: molecular mechanisms and potential targets for treatment. Curr. Mol. Med. 3, 361-372 CrossRef PubMed
66. Yoo, H.Y., Chang, M.S. and Rho, H.M. (1999) Heavy metal-mediated activation of the rat Cu/Zn superoxide dismutase gene via a metal-responsive element. Mol. Gen. Genet. 262, 310-313 CrossRef PubMed
67. Cheng, W.Y., Tong, H., Miller, E.W., Chang, C.J., Remington, J., Zucker, R.M., Bromberg, P.A., Samet, J.M. and Hofer, T.P. (2010) An integrated imaging approach to the study of oxidative stress generation by mitochondrial dysfunction in living cells. Environ. Health Perspect. 118, 902-908 CrossRef PubMed
68. White, R.J. and Reynolds, I.J. (1996) Mitochondrial depolarization in glutamate-stimulated neurons: an early signal specific to excitotoxin exposure. J. Neurosci. 16, 5688-5697 PubMed
69. Kiselyov, K., Jennigs, Jr, J.J., Rbaibi, Y. and Chu, C.T. (2007) Autophagy, mitochondria and cell death in lysosomal storage diseases. Autophagy 3, 259-262 CrossRef PubMed
70. Ventruti, A. and Cuervo, A.M. (2007) Autophagy and neurodegeneration. Curr. Neurol. Neurosci. Rep. 7, 443-451 CrossRef PubMed
71. Spampanato, C., Feeney, E., Li, L., Cardone, M., Lim, J.A., Annunziata, F., Zare, H., Polishchuk, R., Puertollano, R., Parenti, G. et al. (2013) Transcription factor EB (TFEB) is a new therapeutic target for Pompe disease. EMBO. Mol. Med. 5, 691-706 CrossRef PubMed
72. Feeney, E.J., Spampanato, C., Puertollano, R., Ballabio, A., Parenti, G. and Raben, N. (2013) What else is in store for autophagy? Exocytosis of autolysosomes as a mechanism of TFEB-mediated cellular clearance in Pompe disease. Autophagy 9, 1117-1118 CrossRef PubMed
73. Rao, S.K., Huynh, C., Proux-Gillardeaux, V., Galli, T. and Andrews, N.W. (2004) Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis. J. Biol. Chem. 279, 20471-20479 CrossRef PubMed
74. Robinson, N.J. and Winge, D.R. (2010) Copper metallochaperones. Annu. Rev. Biochem. 79, 537-562 CrossRef PubMed
75. Harris, E.D. (2000) Cellular copper transport and metabolism. Annu. Rev. Nutr. 20, 291-310 CrossRef PubMed
76. Caruano-Yzermans, A.L., Bartnikas, T.B. and Gitlin, J.D. (2006) Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase. J. Biol. Chem. 281, 13581-13587 CrossRef PubMed
77. Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y. and Sabatini, D.M. (2011) mTORC1 senses lysosomal amino acids through an inside-out mechanism that requires the vacuolar H(+)-ATPase. Science 334, 678-683 CrossRef PubMed
78. Korolchuk, V.I., Saiki, S., Lichtenberg, M., Siddiqi, F.H., Roberts, E.A., Imarisio, S., Jahreiss, L., Sarkar, S., Futter, M., Menzies, F.M. et al. (2011) Lysosomal positioning coordinates cellular nutrient responses. Nat. Cell. Biol. 13, 453-460 CrossRef PubMed
79. Ma, X., Liu, H., Murphy, J.T., Foyil, S.R., Godar, R.J., Abuirqeba, H., Weinheimer, C.J., Barger, P.M. and Diwan, A. (2015) Regulation of the transcription factor EB-PGC1alpha axis by beclin-1 controls mitochondrial quality and cardiomyocyte death under stress. Mol. Cell. Biol. 35, 956-976 CrossRef PubMed
80. Scott, I., Webster, B.R., Chan, C.K., Okonkwo, J.U., Han, K. and Sack, M.N. (2014) GCN5-like protein 1 (GCN5L1) controls mitochondrial content through coordinated regulation of mitochondrial biogenesis and mitophagy. J. Biol. Chem. 289, 2864-2872 CrossRef PubMed
81. Taniguchi, M., Nadanaka, S., Tanakura, S., Sawaguchi, S., Midori, S., Kawai, Y., Yamaguchi, S., Shimada, Y., Nakamura, Y., Matsumura, Y. et al. (2015) TFE3 Is a bHLH-ZIP-type Transcription Factor that Regulates the Mammalian Golgi Stress Response. Cell Struct. Funct. 40, 13-30 CrossRef PubMed
82. Chen, Y., Azad, M.B. and Gibson, S.B. (2009) Superoxide is the major reactive oxygen species regulating autophagy. Cell Death Differ 16, 1040-1052 CrossRef PubMed
83. Giordano, S., Darley-Usmar, V. and Zhang, J. (2014) Autophagy as an essential cellular antioxidant pathway in neurodegenerative disease. Redox Biol 2, 82-90 CrossRef PubMed
84. Elzi, D.J., Song, M., Hakala, K., Weintraub, S.T. and Shiio, Y. (2014) Proteomic analysis of the EWS-Fli-1 interactome reveals the role of the lysosome in EWS-Fli-1 turnover. In J. Proteome Res., in the press
85. Polito, V.A., Li, H., Martini-Stoica, H., Wang, B., Yang, L., Xu, Y., Swartzlander, D.B., Palmieri, M., di Ronza, A., Lee, V.M. et al. (2014) Selective clearance of aberrant tau proteins and rescue of neurotoxicity by transcription factor EB. EMBO Mol. Med. 6, 1142-1160 CrossRef PubMed
86. Martina, J.A. and Puertollano, R. (2013) Rag GTPases mediate amino acid-dependent recruitment of TFEB and MITF to lysosomes. J. Cell Biol. 200, 475-491 CrossRef PubMed