Importance of cysteine residues in the thyroid hormone transporter MCT8

Endocrinology

Volumn 154, Issue 5, 2013, Pages 1948-1955

  De Souza, Elaine C Lima ^a   Groeneweg, Stefan ^a   Visser, W Edward ^a   Peeters, Robin P ^a   Visser, Theo J ^a  

^a ERASMUS MEDICAL CENTER   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

4 CHLOROMERCURYBENZENESULFONATE; ALANINE; BENZENESULFONIC ACID DERIVATIVE; CYSTEINE; DITHIOTHREITOL; LIOTHYRONINE; MERCURY CHLORIDE; MONOCARBOXYLATE TRANSPORTER 8; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CELL LINE; CONTROLLED STUDY; DRUG INHIBITION; GENE MUTATION; GROWTH INHIBITION; HORMONE TRANSPORT; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

4-CHLOROMERCURIBENZENESULFONATE; ALANINE; AMINO ACID SUBSTITUTION; CELL LINE, TUMOR; CYSTEINE; DITHIOTHREITOL; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; MONOCARBOXYLIC ACID TRANSPORTERS; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; SULFHYDRYL REAGENTS; TIME FACTORS; TRANSFECTION;

EID: 84876772112     PISSN: 00137227     EISSN: 19457170     Source Type: Journal    
DOI: 10.1210/en.2012-2101     Document Type: Article

References (25)

1. Friesema EC, Ganguly S, Abdalla A, et al. Identification of monocarboxylate transporter 8 as a specific thyroid hormone transporter. J Biol Chem. 2003;278:40128-40135.
2. Friesema EC, Visser WE, Visser TJ. Genetics and phenomics of thyroid hormone transport by MCT8. Mol Cell Endocrinol. 2010;322: 107-113.
3. Dumitrescu AM, Liao XH, Best TB, Brockmann K, Refetoff S. A novel syndrome combining thyroid and neurological abnormalities is associated with mutations in a monocarboxylate transporter gene. Am J Hum Genet. 2004;74:168-175.
4. Friesema EC, Grueters A, Biebermann H, et al. Association between mutations in a thyroid hormone transporter and severe X-linked psychomotor retardation. Lancet. 2004;364:1435-1437.
5. Visser WE, Philp NJ, van Dijk TB, et al. Evidence for a homodimeric structure of human monocarboxylate transporter 8. Endocrinology. 2009;150:5163-5170.
6. Giron P, Dayon L, Sanchez JC. Cysteine tagging for MS-based proteomics. Mass Spectrom Rev. 2011;30:366-395.
7. Gruber CW, Cemazar M, Heras B, Martin JL, Craik DJ. Protein disulfide isomerase: the structure of oxidative folding. Trends Biochem Sci. 2006;31:455-464.
8. Trivedi MV, Laurence JS, Siahaan TJ. The role of thiols and disulfides on protein stability. Curr Protein Pept Sci. 2009;10:614-625.
9. Lipton SA, Choi YB, Takahashi H, Zhang D, Li W, Godzik A, Bankston LA. Cysteine regulation of protein function-As exemplified by NMDA-receptor modulation. Trends Neurosci. 2002;25: 474-480.
10. Wilson MC, Meredith D, Fox JE, Manoharan C, Davies AJ, Halestrap AP. Basigin (CD147) is the target for organomercurial inhibition of monocarboxylate transporter isoforms 1 and 4: the ancillary protein for the insensitive MCT2 is EMBIGIN (gp70). J Biol Chem. 2005;280:27213-27221.
11. Kinne A, Kleinau G, Hoefig CS, et al. Essential molecular determinants for thyroid hormone transport and first structural implications for monocarboxylate transporter 8. J Biol Chem. 2010;285: 28054-28063.
12. Kleinau G, Schweizer U, Kinne A, et al. Insights into molecular properties of the human monocarboxylate transporter 8 by combining functional with structural information. Thyroid Res. 2011; 4(Suppl 1):S4.
13. Friesema EC, Kuiper GG, Jansen J, Visser TJ, Kester MH. Thyroid hormone transport by the human monocarboxylate transporter 8 and its rate-limiting role in intracellular metabolism. Mol Endocrinol. 2006;20:2761:2772.
14. López-Corcuera B, Núñez E, Martínez-Maza R, Geerlings A, Aragón C. Substrate-induced conformational changes of extracellular loop 1 in the glycine transporter GLYT2. J Biol Chem. 2001; 276:43463-43470.
15. Hastrup H, Sen N, Javitch JA. The human dopamine transporter forms a tetramer in the plasma membrane: cross-linking of a cysteine in the fourth transmembrane segment is sensitive to cocaine analogs. J Biol Chem. 2003;278:45045-45048.
16. Oppedisano F, Galluccio M, Indiveri C. Inactivation by Hg2-And methylmercury of the glutamine/amino acid transporter (ASCT2) reconstituted in liposomes: Prediction of the involvement of a CXXC motif by homology modelling. Biochem Pharmacol. 2010; 80:1266-1273.
17. Park JS, Hammond Jr. Cysteine residues in the transmembrane (TM) 9 toTM11region of the human equilibrative nucleoside transporter subtype 1 play an important role in inhibitor binding and translocation function. Mol Pharmacol. 2012;82:784-794.
18. ZhaXM,Wang R, CollierDM,Snyder PM, Wemmie JA, Welsh MJ. Oxidant regulated inter-subunit disulfide bond formation between ASIC1a subunits. Proc Natl Acad Sci U S A. 2009;106:3573-3578.
19. Di Cosmo C, Liao XH, Dumitrescu AM, Philp NJ, Weiss RE, Refetoff S. Mice deficient inMCT8reveal a mechanism regulating thyroid hormone secretion. J Clin Invest. 2010;120:3377:3388.
20. Toimela TA, Tähti H. Effects of mercuric chloride exposure on the glutamate uptake by cultured retinal pigment epithelial cells. Toxicol In Vitro. 2001;15:7-12.
21. Mutkus L, Aschner JL, Syversen T, Shanker G, Sonnewald U, Aschner M. Mercuric chloride inhibits the in vitro uptake of glutamate in GLAST-And GLT-1-transfected mutant CHO-K1 cells. Biol Trace Elem Res. 2006;109:267-280.
22. Torres AM, Dnyanmote AV, Bush KT, Wu W, Nigam SK. Deletion of multispecific organic anion transporter Oat1/Slc22a6 protects against mercury-induced kidney injury. J Biol Chem. 2011;286: 26391-26395.
23. Visser WE, Vrijmoeth P, Visser FE, Arts WF, van Toor H, Visser TJ. Identification, functional analysis, prevalence and treatment of monocarboxylate transporter 8 (MCT8) mutations in a cohort of adult patients with mental retardation. Clin Endocrinol (Oxf). 2012;78:310-315.
24. Visser WE, Jansen J, Friesema EC, et al. Novel pathogenic mechanism suggested by ex vivo analysis of MCT8 (SLC16A2) mutations. Hum Mutat. 2009;30:29-38.
25. Falluel-Morel A, Sokolowski K, Sisti HM, Zhou X, Shors TJ, Dicicco-Bloom E. Developmental mercury exposure elicits acute hippocampal cell death, reductions in neurogenesis, and severe learning deficits during puberty. J Neurochem. 2007;103:1968-1981.