F. L. Aachmann, D. E. Fomenko, A. Soragni, V. N. Gladyshev, and A. Dikiy, Solution structure of selenoprotein W and NMR analysis of its interaction with 14-3-3 proteins, J Biol Chem, vol.282, pp.37036-37044, 2007.

J. Ara, S. Przedborski, A. B. Naini, J. , V. Trifiletti et al., Inactivation of tyrosine hydroxylase by nitration following exposure to peroxynitrite and 1-methyl-4-phenyl-1, vol.2, p.6

, Proc Natl Acad Sci U S A, vol.95, pp.7659-7663, 1998.

L. Arodin, A. Miranda-vizuete, P. Swoboda, and A. P. Fernandes, Protective effects of the thioredoxin and glutaredoxin systems in dopamine-induced cell death, Free Radic Biol Med, vol.73, pp.328-336, 2014.

F. P. Bellinger, M. T. Bellinger, L. A. Seale, A. S. Takemoto, A. V. Raman et al., Glutathione peroxidase 4 is associated with neuromelanin in substantia nigra and dystrophic axons in putamen of Parkinson's brain, Mol Neurodegener, vol.6, issue.8, 2011.

F. P. Bellinger, A. V. Raman, M. A. Reeves, and M. J. Berry, Regulation and function of selenoproteins in human disease, Biochem J, vol.422, pp.11-22, 2009.

F. P. Bellinger, A. V. Raman, R. H. Rueli, M. T. Bellinger, A. S. Dewing et al., Changes in selenoprotein P in substantia nigra and putamen in Parkinson's disease, J Parkinsons Dis, vol.2, pp.115-126, 2012.

M. Bisaglia, E. Greggio, M. Beltramini, and L. Bubacco, Dysfunction of dopamine homeostasis: clues in the hunt for novel Parkinson's disease therapies, FASEB J, vol.27, pp.2101-2110, 2013.

B. Blanchard-fillion, D. Prou, M. Polydoro, D. Spielberg, E. Tsika et al., Metabolism of 3-nitrotyrosine induces apoptotic death in dopaminergic cells, J Neurosci, vol.26, pp.6124-6130, 2006.

J. Bové and C. Perier, Neurotoxin-based models of Parkinson's disease, Neuroscience, vol.211, pp.51-76, 2012.

R. E. Burke, O. Malley, and K. , Axon degeneration in Parkinson's disease, Exp Neurol, vol.246, pp.72-83, 2013.

J. R. Cannon, V. M. Tapias, H. M. Na, A. S. Honick, R. E. Drolet et al., A highly reproducible rotenone model of Parkinson's disease, Neurobiol Dis, vol.34, pp.279-290, 2009.

D. S. Cassarino, C. P. Fall, R. H. Swerdlow, T. S. Smith, E. M. Halvorsen et al., Elevated reactive oxygen species and antioxidant enzyme activities in animal and cellular models of Parkinson's disease, Biochim Biophys Acta, vol.1362, pp.77-86, 1997.

M. T. Castex, A. Arabo, M. Bénard, V. Roy, L. Joncour et al., Selenoprotein T deficiency leads to neurodevelopmental abnormalities and hyperactive behavior in mice, Mol Neurobiol, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01783562

S. J. Chinta and J. K. Andersen, Redox imbalance in Parkinson's disease, Biochim Biophys Acta, vol.1780, pp.1362-1367, 2008.

A. Ciesielska, I. Joniec, I. Kurkowska-jastrzebska, A. Cudna, A. Przyby1kowski et al., The impact of age and gender on the striatal astrocytes activation in murine model of Parkinson's disease, Inflamm Res, vol.58, pp.747-753, 2009.

M. Conrad, C. Jakupoglu, S. G. Moreno, S. Lippl, A. Banjac et al.,

M. Brielmeier, Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function, Mol Cell Biol, vol.24, pp.9414-9423, 2004.

L. M. De-lau and M. M. Breteler, Epidemiology of Parkinson's disease, Lancet Neurol, vol.5, pp.525-535, 2006.

R. M. Deacon, Measuring motor coordination in mice, J Vis Exp, vol.75, pp.1-8, 2013.

A. Dikiy, S. V. Novoselov, D. E. Fomenko, A. Sengupta, B. A. Carlson et al., SelW, SelH, and Rdx12: genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family, Biochem J, vol.46, pp.6871-6882, 2007.

S. M. Fleming, C. Zhu, P. O. Fernagut, A. Mehta, C. D. Dicarlo et al., Behavioral and immunohistochemical effects of chronic intravenous and subcutaneous infusions of varying doses of rotenone, Exp Neurol, vol.187, pp.418-429, 2004.

C. Gibrat, M. Saint-pierre, M. Bousquet, D. Lévesque, C. Rouillard et al., Differences between subacute and chronic MPTP mice models: investigation of dopaminergic neuronal degeneration and alpha-synuclein inclusion, J Neurochem, vol.109, pp.1469-1482, 2009.

J. A. Goldberg, J. N. Guzman, C. M. Estep, E. Ilijic, J. Kondapalli et al., Calcium entry induces mitochondrial oxidant stress in vagal neurons at risk in Parkinson's disease, Nat Neurosci, vol.15, pp.1414-1421, 2012.

L. Grumolato, H. Ghzili, M. Montero-hadjadje, S. Gasman, J. Lesage et al., Selenoprotein T is a PACAP-regulated gene involved in intracellular Ca2+ mobilization and neuroendocrine secretion, FASEB J, vol.22, pp.1756-1768, 2008.
URL : https://hal.archives-ouvertes.fr/hal-01962747

L. Grumolato, G. Liu, P. Mong, R. Mudbhary, R. Biswas et al., Canonical and noncanonical Wnts use a common mechanism to activate completely unrelated coreceptors, Genes Dev, vol.24, pp.2517-2530, 2010.

D. L. Hatfield, P. A. Tsuji, B. A. Carlson, and G. Vn, Selenium and selenocysteine: roles in cancer, health and development, Trends Biochem Sci, vol.39, pp.112-120, 2014.

O. Hwang, Role of oxidative stress in Parkinson's disease, Exp Neurobiol, vol.22, pp.11-17, 2013.

H. Ischiropoulos, Biological selectivity and functional aspects of protein tyrosine nitration, Biochem Biophys Res Commun, vol.305, pp.776-783, 2003.

C. Jakupoglu, G. Przemeck, M. Schneider, S. G. Moreno, N. Mayr et al., Cytoplasmic thioredoxin reductase is essential for embryogenesis but dispensable for cardiac development, Mol Cell Biol, vol.25, 1980.

P. Jenner, A. H. Schapira, and C. D. Marsden, New insights into the cause of Parkinson's disease, Neurology, vol.42, pp.2241-2250, 1992.

P. Klivenyi, O. A. Andreassen, R. J. Ferrante, A. Dedeoglu, G. Mueller et al., Mice deficient in cellular glutathione peroxidase show increased vulnerability to malonate, 3-nitropropionic acid, and 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine, J Neurosci, vol.20, pp.1-7, 2000.

M. Kohutnicka, E. Lewandowska, I. Kurkowska-jastrzebska, and A. Cz1onkowski, Microglial and astro-2,3,6-tetrahydropyridine (MPTP), Immunopharmacology, vol.39, pp.167-180, 1998.

G. V. Kryukov, V. M. Kryukov, and G. Vn, New mammalian selenocysteine-containing proteins identified with an algorithm that searches for selenocysteine insertion sequence elements, J Biol Chem, vol.274, pp.33888-33897, 1999.

V. M. Labunskyy, M. H. Yoo, D. L. Hatfield, and G. Vn, Sep15, a thioredoxin-like selenoprotein, is involved in the unfolded protein response and differentially regulated by adaptive and acute ER stresses, Biochemistry, vol.48, pp.8458-8465, 2009.

S. Lee, S. M. Kim, and L. Rt, Thioredoxin and thioredoxin target proteins: from molecular mechanisms to functional significance, Antioxid Redox Signal, vol.18, pp.1165-1207, 2013.

A. J. Lees, J. Hardy, and R. T. , Parkinson's disease. Lancet, vol.373, pp.2055-2066, 2009.

M. T. Lin and M. F. Beal, Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases, Nature, vol.443, pp.787-795, 2006.

P. Lopert, B. J. Day, and P. M. , Thioredoxin reductase deficiency potentiates oxidative stress, mitochondrial dysfunction and cell death in dopaminergic cells, PLoS One, vol.7, p.50683, 2012.

J. Lotharious and P. Brundin, Pathogenesis of Parkinson's disease: dopamine, vesicles and a-synuclein, Nature, vol.3, pp.932-942, 2002.

L. Holmgren and A. , Rat liver thioredoxin and thioredoxin reductase: purification and characterization, Biochemistry, vol.21, pp.6628-6633, 1982.

S. Marchi, C. Giorgi, J. M. Suski, C. Agnoletto, A. Bononi et al., Mitochondria-ros crosstalk in the control of cell death and aging, J Signal Transduct, p.329635, 2012.

J. A. Obeso, M. C. Rodriguez-oroz, C. G. Goetz, C. Marin, J. H. Kordower et al., Missing pieces in the Parkinson's disease puzzle, Nat Med, vol.16, pp.653-661, 2010.

G. Prevost, A. Arabo, L. Jian, E. Quelennec, D. Cartier et al., The PACAPregulated gene selenoprotein T is abundantly expressed in mouse and human beta-cells and its targeted inactivation impairs glucose tolerance, Endocrinology, vol.154, pp.3796-3806, 2013.

M. P. Rayman, Selenium and human health, Lancet, vol.379, pp.1256-1268, 2012.

J. Sanchez-ramos, J. N. Barrett, M. Goldstein, W. J. Weiner, and H. F. , 1-Methyl-4-phenylpyridinium (MPP+) but not 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) selectively destroys dopaminergic neurons in cultures of dissociated rat mesencephalic neurons, Neurosci Lett, vol.12, pp.215-220, 1986.

A. Schapira, Mitochondria in the aetiology and pathogenesis of Parkinson's disease, Lancet Neurol, vol.7, pp.97-109, 2008.

W. Schultz, Predictive reward signal of dopamine neurons, J Neurophysiol, vol.80, pp.1-27, 1998.

S. Seeher, B. A. Carlson, A. C. Miniard, E. K. Wirth, Y. Mahdi et al., Impaired selenoprotein expression in brain triggers striatal neuronal loss leading to coordination defects in mice, Biochem J, vol.462, pp.67-75, 2014.

A. Sengupta, B. A. Carlson, V. M. Labunskyy, V. N. Gladyshev, and D. L. Hatfield, Selenoprotein T deficiency alters cell adhesion and elevates selenoprotein W expression in murine fibroblast cells, Biochem Cell Biol, vol.87, pp.953-961, 2009.

V. A. Shchedrina, R. A. Everley, Y. Zhang, S. P. Gygi, D. L. Hatfield et al., Selenoprotein K binds multiprotein complexes and is involved in the regulation of endoplasmic reticulum homeostasis, J Biol Chem, vol.286, pp.42937-42948, 2011.

G. K. Shinomol, R. B. Mythri, S. Bharath, M. M. , and M. , Bacopa monnieri extract offsets rotenone-induced cytotoxicity in dopaminergic cells and oxidative impairments in mice brain, Cell Mol Neurobiol, vol.32, pp.455-465, 2012.

J. Soerensen, C. Jakupoglu, H. Beck, H. Förster, J. Schmidt et al., The role of thioredoxin reductases in brain development, PLoS One, vol.3, p.1813, 2008.

S. R. Subramaniam and M. F. Chesselet, Mitochondrial dysfunction and oxidative stress in Parkinson's disease, Prog Neurobiol, vol.106, pp.17-32, 2013.

Y. Tanguy, A. Falluel-morel, S. Arthaud, L. Boukhzar, D. L. Manecka et al., The PACAP-regulated gene selenoprotein T is highly induced in nervous, endocrine, and metabolic tissues during ontogenetic and regenerative processes, Endocrinology, vol.152, pp.4322-4335, 2011.
URL : https://hal.archives-ouvertes.fr/hal-00682913

P. Teismann and J. B. Schulz, Cellular pathology of Parkinson's disease: astrocytes, microglia and inflammation, Cell Tissue Res, vol.318, pp.149-161, 2004.

B. Thomas and M. F. Beal, Parkinson's disease, Hum Mol Genet, vol.2, pp.183-194, 2007.

F. Tronche, C. Kellendonk, O. Kretz, P. Gass, K. Anlag et al., Disruption of the glucocorticoid receptor gene in the nervous system results in reduced anxiety, Nat Genet, vol.23, pp.99-103, 1999.

W. M. Valentine, T. W. Abel, K. E. Hill, L. M. Austin, and R. F. Burk, Neurodegeneration in mice resulting from loss of fonctional selenoprotein P or its receptor apolipoprotein E receptor 2, J Neuropathol Exp Neurol, vol.67, pp.68-77, 2008.

D. Viggiano, D. Vallone, and A. Sadile, Dysfunctions in dopamine systems and ADHD: evidence from animals and modeling, Neural Plast, vol.11, pp.97-114, 2004.

E. K. Wirth, M. Conrad, J. Winterer, C. Wozny, B. A. Carlson et al., Address correspondence to: Dr. Youssef Anouar Laboratory of Neuronal and Neuroendocrine Differentiation and Communication Inserm U982, FASEB J, vol.24, pp.844-852, 2010.

, France E-mail: youssef.anouar@univ-rouen.fr Date of first submission to ARS Central, 2015.

E. Varlamova, Protein-protein interactions of ER-resident selenoproteins with their physiological partners, Biochimie, vol.171, issue.172, pp.197-204, 2020.

M. Conrad and B. Proneth, Selenium: Tracing Another Essential Element of Ferroptotic Cell Death, Cell Chemical Biology, vol.27, pp.409-419, 2020.

S. J. Elias and . Arnér, Common modifications of selenocysteine in selenoproteins, Essays in Biochemistry, vol.64, issue.1, pp.45-53, 2020.

F. Maass, B. Michalke, D. Willkommen, A. Leha, C. Schulte et al., Elemental fingerprint: Reassessment of a cerebrospinal fluid biomarker for Parkinson's disease, Neurobiology of Disease, vol.134, 2020.

D. Santesmasses, M. Mariotti, N. Vadim, and . Gladyshev, Tolerance to Selenoprotein Loss Differs between Human and Mouse, Molecular Biology and Evolution, vol.37, issue.2, pp.341-354, 2020.

F. Maass, B. Michalke, D. Willkommen, C. Schulte, L. Tönges et al., Selenium speciation analysis in the cerebrospinal fluid of patients with Parkinson's disease, Journal of Trace Elements in Medicine and Biology, vol.57, 2020.

Z. Shao, X. Zhang, H. Fan, X. Wang, H. Wu et al.,

, Selenoprotein T Promotes Proliferation and G1-to-S Transition in SK-N-SH Cells: Implications in Parkinson's Disease, vol.149, pp.2110-2119

A. Leonardi, S. Evke, M. Lee, J. A. Melendez, and T. J. Begley, Epitranscriptomic systems regulate the translation of reactive oxygen species detoxifying and disease linked selenoproteins, Free Radical Biology and Medicine, vol.143, pp.573-593, 2019.

C. Rocca, T. Pasqua, L. Boukhzar, Y. Anouar, and T. Angelone, Progress in the emerging role of selenoproteins in cardiovascular disease: focus on endoplasmic reticulum-resident selenoproteins, Cellular and Molecular Life Sciences, vol.76, issue.20, pp.3969-3985, 2019.

S. Prem-prakash-kushwaha, A. Gupta, S. Singh, and . Kumar, Emerging Role of Migration and Invasion Enhancer 1 (MIEN1) in Cancer Progression and Metastasis. Frontiers in Oncology 9, 2019.

H. Abid, D. Cartier, A. Hamieh, A. François-bellan, C. Bucharles et al., AMPK Activation of PGC-1?/NRF-1-Dependent SELENOT Gene Transcription Promotes PACAP-Induced Neuroendocrine Cell Differentiation Through Tolerance to Oxidative Stress, Molecular Neurobiology, vol.56, issue.6, pp.4086-4101, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02093045

X. Zhang, R. Liu, W. Cheng, and J. Zhu, Prioritized brain selenium retention and selenoprotein expression: Nutritional insights into Parkinson's disease, Mechanisms of Ageing and Development, vol.180, pp.89-96, 2019.

J. Hwang-lee, J. K. Jang, Y. Kwan, Y. Ko, M. Jin et al., Degradation of selenoprotein S and selenoprotein K through PPAR?-mediated ubiquitination is required for adipocyte differentiation, Cell Death & Differentiation, vol.26, issue.6, pp.1007-1023, 2019.

L. Zhang, J. Zhu, X. Zhang, and W. Cheng, The Thioredoxin-Like Family of Selenoproteins: Implications in Aging and Age-Related Degeneration, Biological Trace Element Research, vol.188, issue.1, pp.189-195, 2019.

M. Daniela, K. Sakari, and K. Thomas, Hypoxia and Reactive Oxygen Species as Modulators of Endoplasmic Reticulum and Golgi Homeostasis, Antioxidants & Redox Signaling, vol.30, issue.1, pp.113-137, 2019.

L. Guo, W. Yang, Q. Huang, J. Qiang, J. R. Hart et al., Selenocysteine-Specific Mass Spectrometry Reveals Tissue-Distinct Selenoproteomes and Candidate Selenoproteins, Cell Chemical Biology, vol.25, issue.11, pp.1380-1388, 2018.

J. Pedro-friedmann, M. Angeli, and . Conrad, Selenium and GPX4, a vital symbiosis, Free Radical Biology and Medicine, vol.127, pp.153-159, 2018.

Y. Anouar, I. Lihrmann, A. Falluel-morel, and L. Boukhzar, Selenoprotein T is a key player in ER proteostasis, endocrine homeostasis and neuroprotection, Free Radical Biology and Medicine, vol.127, pp.145-152, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02427048

J. Avery and P. Hoffmann, Selenium, Selenoproteins, and Immunity, vol.10, 1203.

G. Krishna and . Muralidhara, Oral supplements of inulin during gestation offsets rotenone-induced oxidative impairments and neurotoxicity in maternal and prenatal rat brain, Biomedicine & Pharmacotherapy, vol.104, pp.751-762, 2018.

C. Rocca, L. Boukhzar, M. C. Granieri, I. Alsharif, R. Mazza et al., A selenoprotein T-derived peptide protects the heart against ischaemia/reperfusion injury through inhibition of apoptosis and oxidative stress, Acta Physiologica, vol.223, issue.4, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01939294

C. L. Hawkins, A therapeutic role for selenoprotein T in reducing ischaemia/reperfusion injury in the heart?, Acta Physiologica, vol.223, issue.4, 2018.

M. E. Johnson, M. F. Salvatore, S. A. Maiolo, and L. Bobrovskaya, Tyrosine hydroxylase as a sentinel for central and peripheral tissue responses in Parkinson's progression: Evidence from clinical studies and neurotoxin models, Progress in Neurobiology, vol.165, pp.1-25, 2018.

J. Zhou, C. Li, G. Gu, Q. Wang, and M. Guo, Selenoprotein N Was Required for the Regulation of Selenium on the Uterine Smooth Muscle Contraction in Mice, Biological Trace Element Research, vol.183, issue.1, pp.138-146, 2018.

E. Zoidis and I. Seremelis, Selenium-Dependent Antioxidant Enzymes: Actions and Properties of Selenoproteins, Antioxidants, vol.7, issue.5, 2018.

M. W. Pitts and P. R. Hoffmann, Endoplasmic reticulum-resident selenoproteins as regulators of calcium signaling and homeostasis, Cell Calcium, vol.70, pp.76-86, 2018.

Y. Liu, X. Guo, T. Hirata, Y. Rong, D. Motooka et al., N-Glycan-dependent protein folding and endoplasmic reticulum retention regulate GPI-anchor processing, Journal of Cell Biology, vol.217, issue.2, pp.585-599, 2018.

J. Zhou, J. Zhou, L. Su, and K. Huang, Xin Gen Lei. Selenium and Diabetes, pp.317-344

N. Fradejas-villar and U. Schweizer, Selenium and Neurodevelopment 177-192

A. Hamieh, D. Cartier, H. Abid, A. Calas, C. Burel et al., Selenoprotein T is a novel OST subunit that regulates UPR signaling and hormone secretion, EMBO reports, vol.18, issue.11, pp.1935-1946, 2017.
URL : https://hal.archives-ouvertes.fr/inserm-01614090

L. Romanelli-cedrez, I. Carrera, L. Otero, A. Miranda-vizuete, M. Mariotti et al.,

, Selenoprotein T is required for pathogenic bacteria avoidance in Caenorhabditis elegan s, Free Radical Biology and Medicine, vol.108, pp.174-182

E. Ferrari, A. Capucciati, I. Prada, F. A. Zucca, D. Giulia et al., Structure Characterization, and Evaluation in Microglia Cultures of Neuromelanin Analogues Suitable for Modeling Parkinson's Disease, vol.8, pp.501-512, 2017.

W. Chen, Z. Zhang, F. Yan, X. Jiang, S. Qin et al., Identification of three selenoprotein T paralogs in goldfish (Carassius auratus) and expression analysis in response to environmental stressors, Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, vol.203, pp.65-75, 2017.

L. Boukhzar, Y. Tanguy, H. Abid, M. Castex, A. Hamieh et al., Selenoprotein T: From Discovery to Functional Studies Using Conditional Knockout Mice 275-286

U. Schweizer, Selenoproteins in Nervous System Development, Function and Degeneration 427-439