메뉴 건너뛰기




Volumn 1808, Issue 1, 2011, Pages 65-77

Characterisation of the purified human sodium/iodide symporter reveals that the protein is mainly present in a dimeric form and permits the detailed study of a native C-terminal fragment

Author keywords

Eukaryote; Membrane protein; Oligomeric state; Post translational regulation; Sodium iodide symporter; Thyroid

Indexed keywords

COMPLEMENTARY DNA; SODIUM IODIDE SYMPORTER;

EID: 78649803019     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.08.013     Document Type: Article
Times cited : (19)

References (55)
  • 2
    • 0035425520 scopus 로고    scopus 로고
    • Journey of the iodide transporter NIS: From its molecular identification to its clinical role in cancer
    • C. Riedel, O. Dohan, A. De la Vieja, C.S. Ginter, and N. Carrasco Journey of the iodide transporter NIS: from its molecular identification to its clinical role in cancer Trends Biochem. Sci. 26 2001 490 496
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 490-496
    • Riedel, C.1    Dohan, O.2    De La Vieja, A.3    Ginter, C.S.4    Carrasco, N.5
  • 4
    • 0036425965 scopus 로고    scopus 로고
    • The sodium iodide symporter: Its pathophysiological and therapeutic implications
    • C. Spitzweg, and J.C. Morris The sodium iodide symporter: its pathophysiological and therapeutic implications Clin. Endocrinol. 57 2002 559 574 (Oxf)
    • (2002) Clin. Endocrinol. , vol.57 , pp. 559-574
    • Spitzweg, C.1    Morris, J.C.2
  • 5
    • 0033922682 scopus 로고    scopus 로고
    • Molecular analysis of the sodium/iodide symporter: Impact on thyroid and extrathyroid pathophysiology
    • A. De La Vieja, O. Dohan, O. Levy, and N. Carrasco Molecular analysis of the sodium/iodide symporter: impact on thyroid and extrathyroid pathophysiology Physiol. Rev. 80 2000 1083 1105
    • (2000) Physiol. Rev. , vol.80 , pp. 1083-1105
    • De La Vieja, A.1    Dohan, O.2    Levy, O.3    Carrasco, N.4
  • 6
    • 0030053759 scopus 로고    scopus 로고
    • Cloning and characterization of the thyroid iodide transporter
    • G. Dai, O. Levy, and N. Carrasco Cloning and characterization of the thyroid iodide transporter Nature 379 1996 458 460
    • (1996) Nature , vol.379 , pp. 458-460
    • Dai, G.1    Levy, O.2    Carrasco, N.3
  • 8
    • 0034913576 scopus 로고    scopus 로고
    • Cloning of the mouse sodium iodide symporter and its expression in the mammary gland and other tissues
    • B. Perron, A.M. Rodriguez, G. Leblanc, and T. Pourcher Cloning of the mouse sodium iodide symporter and its expression in the mammary gland and other tissues J. Endocrinol. 170 2001 185 196
    • (2001) J. Endocrinol. , vol.170 , pp. 185-196
    • Perron, B.1    Rodriguez, A.M.2    Leblanc, G.3    Pourcher, T.4
  • 9
    • 0037010179 scopus 로고    scopus 로고
    • The sodium/substrate symporter family: Structural and functional features
    • H. Jung The sodium/substrate symporter family: structural and functional features FEBS Lett. 529 2002 73 77
    • (2002) FEBS Lett. , vol.529 , pp. 73-77
    • Jung, H.1
  • 10
    • 0032575638 scopus 로고    scopus 로고
    • N-linked glycosylation of the thyroid Na+/I- symporter (NIS). Implications for its secondary structure model
    • O. Levy, A. De la Vieja, C.S. Ginter, C. Riedel, G. Dai, and N. Carrasco N-linked glycosylation of the thyroid Na+/I- symporter (NIS). Implications for its secondary structure model J. Biol. Chem. 273 1998 22657 22663
    • (1998) J. Biol. Chem. , vol.273 , pp. 22657-22663
    • Levy, O.1    De La Vieja, A.2    Ginter, C.S.3    Riedel, C.4    Dai, G.5    Carrasco, N.6
  • 11
    • 0035877782 scopus 로고    scopus 로고
    • Post-transcriptional regulation of the sodium/iodide symporter (NIS) by thyrotropin
    • C. Riedel, O. Levy, and N. Carrasco Post-transcriptional regulation of the sodium/iodide symporter (NIS) by thyrotropin J. Biol. Chem. 276 2001 21458 21463
    • (2001) J. Biol. Chem. , vol.276 , pp. 21458-21463
    • Riedel, C.1    Levy, O.2    Carrasco, N.3
  • 13
    • 37549070369 scopus 로고    scopus 로고
    • Identification of in vivo phosphorylation sites and their functional significance in the sodium iodide symporter
    • D.D. Vadysirisack, E.S. Chen, Z. Zhang, M.D. Tsai, G.D. Chang, and S.M. Jhiang Identification of in vivo phosphorylation sites and their functional significance in the sodium iodide symporter J. Biol. Chem. 282 2007 36820 36828
    • (2007) J. Biol. Chem. , vol.282 , pp. 36820-36828
    • Vadysirisack, D.D.1    Chen, E.S.2    Zhang, Z.3    Tsai, M.D.4    Chang, G.D.5    Jhiang, S.M.6
  • 14
    • 34547808829 scopus 로고    scopus 로고
    • MEK signaling modulates sodium iodide symporter at multiple levels and in a paradoxical manner
    • D.D. Vadysirisack, A. Venkateswaran, Z. Zhang, and S.M. Jhiang MEK signaling modulates sodium iodide symporter at multiple levels and in a paradoxical manner Endocr Relat Cancer 14 2007 421 432
    • (2007) Endocr Relat Cancer , vol.14 , pp. 421-432
    • Vadysirisack, D.D.1    Venkateswaran, A.2    Zhang, Z.3    Jhiang, S.M.4
  • 15
    • 56849115726 scopus 로고    scopus 로고
    • Phosphoinositide-3-kinase inhibition induces sodium/iodide symporter expression in rat thyroid cells and human papillary thyroid cancer cells
    • T. Kogai, S. Sajid-Crockett, L.S. Newmarch, Y.Y. Liu, and G.A. Brent Phosphoinositide-3-kinase inhibition induces sodium/iodide symporter expression in rat thyroid cells and human papillary thyroid cancer cells J. Endocrinol. 199 2008 243 252
    • (2008) J. Endocrinol. , vol.199 , pp. 243-252
    • Kogai, T.1    Sajid-Crockett, S.2    Newmarch, L.S.3    Liu, Y.Y.4    Brent, G.A.5
  • 17
    • 34748836984 scopus 로고    scopus 로고
    • Quaternary structure and apical membrane sorting of the mammalian NaSi-1 sulfate transporter in renal cell lines
    • R.R. Regeer, A. Nicke, and D. Markovich Quaternary structure and apical membrane sorting of the mammalian NaSi-1 sulfate transporter in renal cell lines Int. J. Biochem. Cell Biol. 39 2007 2240 2251
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 2240-2251
    • Regeer, R.R.1    Nicke, A.2    Markovich, D.3
  • 18
    • 34548107626 scopus 로고    scopus 로고
    • Regions in the cytosolic C-terminus of the secretory Na(+)-K(+)-2Cl(-) co-transporter NKCC1 are required for its homodimerization
    • M.N. Parvin, T. Gerelsaikhan, and R.J. Turner Regions in the cytosolic C-terminus of the secretory Na(+)-K(+)-2Cl(-) co-transporter NKCC1 are required for its homodimerization Biochemistry 46 2007 9630 9637
    • (2007) Biochemistry , vol.46 , pp. 9630-9637
    • Parvin, M.N.1    Gerelsaikhan, T.2    Turner, R.J.3
  • 20
    • 0028101308 scopus 로고
    • Evidence that Na+/H + exchanger isoforms NHE1 and NHE3 exist as stable dimers in membranes with a high degree of specificity for homodimers
    • P. Fafournoux, J. Noel, and J. Pouyssegur Evidence that Na+/H + exchanger isoforms NHE1 and NHE3 exist as stable dimers in membranes with a high degree of specificity for homodimers J. Biol. Chem. 269 1994 2589 2596
    • (1994) J. Biol. Chem. , vol.269 , pp. 2589-2596
    • Fafournoux, P.1    Noel, J.2    Pouyssegur, J.3
  • 21
    • 1942532338 scopus 로고    scopus 로고
    • New insights into the structure and oligomeric state of the bacterial multidrug transporter EmrE: An unusual asymmetric homo-dimer
    • I. Ubarretxena-Belandia, and C.G. Tate New insights into the structure and oligomeric state of the bacterial multidrug transporter EmrE: an unusual asymmetric homo-dimer FEBS Lett. 564 2004 234 238
    • (2004) FEBS Lett. , vol.564 , pp. 234-238
    • Ubarretxena-Belandia, I.1    Tate, C.G.2
  • 22
    • 52449096621 scopus 로고    scopus 로고
    • The dimeric form of Ca2 + -ATPase is involved in Ca2+ transport in the sarcoplasmic reticulum
    • M. Ushimaru, and Y. Fukushima The dimeric form of Ca2 + -ATPase is involved in Ca2+ transport in the sarcoplasmic reticulum Biochem. J. 414 2008 357 361
    • (2008) Biochem. J. , vol.414 , pp. 357-361
    • Ushimaru, M.1    Fukushima, Y.2
  • 23
    • 2542461709 scopus 로고    scopus 로고
    • Sodium-dependent neurotransmitter transporters: Oligomerization as a determinant of transporter function and trafficking
    • H.H. Sitte, H. Farhan, and J.A. Javitch Sodium-dependent neurotransmitter transporters: oligomerization as a determinant of transporter function and trafficking Mol. Interv. 4 2004 38 47
    • (2004) Mol. Interv. , vol.4 , pp. 38-47
    • Sitte, H.H.1    Farhan, H.2    Javitch, J.A.3
  • 24
    • 33947369500 scopus 로고    scopus 로고
    • G protein-coupled receptor dimerisation: Molecular basis and relevance to function
    • G. Milligan G protein-coupled receptor dimerisation: molecular basis and relevance to function Biochim. Biophys. Acta 1768 2007 825 835
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 825-835
    • Milligan, G.1
  • 26
    • 27744455336 scopus 로고    scopus 로고
    • Cell surface targeting accounts for the difference in iodide uptake activity between human Na+/I- symporter and rat Na+/I- symporter
    • Z. Zhang, Y.Y. Liu, and S.M. Jhiang Cell surface targeting accounts for the difference in iodide uptake activity between human Na+/I- symporter and rat Na+/I- symporter J. Clin. Endocrinol. Metab. 90 2005 6131 6140
    • (2005) J. Clin. Endocrinol. Metab. , vol.90 , pp. 6131-6140
    • Zhang, Z.1    Liu, Y.Y.2    Jhiang, S.M.3
  • 28
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 29
    • 23644444909 scopus 로고    scopus 로고
    • Refractive index-based determination of detergent concentration and its application to the study of membrane proteins
    • P. Strop, and A.T. Brunger Refractive index-based determination of detergent concentration and its application to the study of membrane proteins Protein Sci. 14 2005 2207 2211
    • (2005) Protein Sci. , vol.14 , pp. 2207-2211
    • Strop, P.1    Brunger, A.T.2
  • 31
    • 0024321837 scopus 로고
    • Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography
    • Y. Hayashi, H. Matsui, and T. Takagi Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography Methods Enzymol. 172 1989 514 528
    • (1989) Methods Enzymol. , vol.172 , pp. 514-528
    • Hayashi, Y.1    Matsui, H.2    Takagi, T.3
  • 32
    • 0033021364 scopus 로고    scopus 로고
    • Charge translocation by the Na+/K + -ATPase investigated on solid supported membranes: Rapid solution exchange with a new technique
    • J. Pintschovius, and K. Fendler Charge translocation by the Na+/K + -ATPase investigated on solid supported membranes: rapid solution exchange with a new technique Biophys. J. 76 1999 814 826
    • (1999) Biophys. J. , vol.76 , pp. 814-826
    • Pintschovius, J.1    Fendler, K.2
  • 35
    • 0033061571 scopus 로고    scopus 로고
    • Initiation of translation in prokaryotes and eukaryotes
    • M. Kozak Initiation of translation in prokaryotes and eukaryotes Gene 234 1999 187 208
    • (1999) Gene , vol.234 , pp. 187-208
    • Kozak, M.1
  • 37
    • 17044424577 scopus 로고    scopus 로고
    • Sites of proteolytic processing and noncovalent association of the distal C-terminal domain of CaV1.1 channels in skeletal muscle
    • J.T. Hulme, K. Konoki, T.W. Lin, M.A. Gritsenko, D.G. Camp 2nd, D.J. Bigelow, and W.A. Catterall Sites of proteolytic processing and noncovalent association of the distal C-terminal domain of CaV1.1 channels in skeletal muscle Proc. Natl Acad. Sci. USA 102 2005 5274 5279
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 5274-5279
    • Hulme, J.T.1    Konoki, K.2    Lin, T.W.3    Gritsenko, M.A.4    Camp II, D.G.5    Bigelow, D.J.6    Catterall, W.A.7
  • 39
    • 0029888217 scopus 로고    scopus 로고
    • Phosphate deprivation induces overexpression of two proteins related to the rat renal phosphate co-transporter NaPi-2
    • C.J. Boyer, Y. Xiao, A. Dugre, E. Vincent, M.C. Delisle, and R. Beliveau Phosphate deprivation induces overexpression of two proteins related to the rat renal phosphate co-transporter NaPi-2 Biochim. Biophys. Acta 1281 1996 117 123
    • (1996) Biochim. Biophys. Acta , vol.1281 , pp. 117-123
    • Boyer, C.J.1    Xiao, Y.2    Dugre, A.3    Vincent, E.4    Delisle, M.C.5    Beliveau, R.6
  • 40
    • 0030971208 scopus 로고    scopus 로고
    • Involvement of disulphide bonds in the renal sodium/phosphate co-transporter NaPi-2
    • Y. Xiao, C.J. Boyer, E. Vincent, A. Dugre, V. Vachon, M. Potier, and R. Beliveau Involvement of disulphide bonds in the renal sodium/phosphate co-transporter NaPi-2 Biochem. J. 323 Pt 2 1997 401 408
    • (1997) Biochem. J. , vol.323 , Issue.PART 2 , pp. 401-408
    • Xiao, Y.1    Boyer, C.J.2    Vincent, E.3    Dugre, A.4    Vachon, V.5    Potier, M.6    Beliveau, R.7
  • 41
    • 4544338200 scopus 로고    scopus 로고
    • State of the Escherichia coli metal transporter YiiP
    • Y. Wei, H. Li, and D.Fu. Oligomeric state of the Escherichia coli metal transporter YiiP J. Biol. Chem. 279 2004 39251 39259
    • (2004) J. Biol. Chem. , vol.279 , pp. 39251-39259
    • Wei, Y.1    Li, H.2    Oligomeric, D.Fu.3
  • 42
    • 0242424106 scopus 로고    scopus 로고
    • Trimeric subunit stoichiometry of the glutamate transporters from Bacillus caldotenax and Bacillus stearothermophilus
    • D. Yernool, O. Boudker, E. Folta-Stogniew, and E. Gouaux Trimeric subunit stoichiometry of the glutamate transporters from Bacillus caldotenax and Bacillus stearothermophilus Biochemistry 42 2003 12981 12988
    • (2003) Biochemistry , vol.42 , pp. 12981-12988
    • Yernool, D.1    Boudker, O.2    Folta-Stogniew, E.3    Gouaux, E.4
  • 44
  • 45
    • 0025310534 scopus 로고
    • In vivo expression of the lacY gene in two segments leads to functional lac permease
    • E. Bibi, and H.R. Kaback In vivo expression of the lacY gene in two segments leads to functional lac permease Proc. Natl Acad. Sci. USA 87 1990 4325 4329
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4325-4329
    • Bibi, E.1    Kaback, H.R.2
  • 46
    • 0030010702 scopus 로고    scopus 로고
    • In vivo membrane assembly of split variants of the E.coli outer membrane protein OmpA
    • R. Koebnik In vivo membrane assembly of split variants of the E.coli outer membrane protein OmpA EMBO J. 15 1996 3529 3537
    • (1996) EMBO J. , vol.15 , pp. 3529-3537
    • Koebnik, R.1
  • 47
    • 0030838729 scopus 로고    scopus 로고
    • Reconstitution of functional voltage-gated chloride channels from complementary fragments of CLC-1
    • T. Schmidt-Rose, and T.J. Jentsch Reconstitution of functional voltage-gated chloride channels from complementary fragments of CLC-1 J. Biol. Chem. 272 1997 20515 20521
    • (1997) J. Biol. Chem. , vol.272 , pp. 20515-20521
    • Schmidt-Rose, T.1    Jentsch, T.J.2
  • 48
    • 0032589157 scopus 로고    scopus 로고
    • An engineered cytochrome b6c1 complex with a split cytochrome b is able to support photosynthetic growth of Rhodobacter capsulatus
    • A.S. Saribas, S. Mandaci, and F. Daldal An engineered cytochrome b6c1 complex with a split cytochrome b is able to support photosynthetic growth of Rhodobacter capsulatus J. Bacteriol. 181 1999 5365 5372
    • (1999) J. Bacteriol. , vol.181 , pp. 5365-5372
    • Saribas, A.S.1    Mandaci, S.2    Daldal, F.3
  • 49
    • 0034714356 scopus 로고    scopus 로고
    • Characterization of the Vibrio parahaemolyticus Na+/Glucose co-transporter. A bacterial member of the sodium/glucose transporter (SGLT) family
    • Z. Xie, E. Turk, and E.M. Wright Characterization of the Vibrio parahaemolyticus Na+/Glucose co-transporter. A bacterial member of the sodium/glucose transporter (SGLT) family J. Biol. Chem. 275 2000 25959 25964
    • (2000) J. Biol. Chem. , vol.275 , pp. 25959-25964
    • Xie, Z.1    Turk, E.2    Wright, E.M.3
  • 50
    • 0035374625 scopus 로고    scopus 로고
    • Split Na + -Ca2+ exchangers. Implications for function and expression
    • M. Ottolia, S. John, Z. Qiu, and K.D. Philipson Split Na + -Ca2+ exchangers. Implications for function and expression J. Biol. Chem. 276 2001 19603 19609
    • (2001) J. Biol. Chem. , vol.276 , pp. 19603-19609
    • Ottolia, M.1    John, S.2    Qiu, Z.3    Philipson, K.D.4
  • 51
  • 52
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • A. Bachmair, D. Finley, and A. Varshavsky In vivo half-life of a protein is a function of its amino-terminal residue Science 234 1986 179 186
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 53
    • 35548974677 scopus 로고    scopus 로고
    • The mammalian N-end rule pathway: New insights into its components and physiological roles
    • T. Tasaki, and Y.T. Kwon The mammalian N-end rule pathway: new insights into its components and physiological roles Trends Biochem. Sci. 32 2007 520 528
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 520-528
    • Tasaki, T.1    Kwon, Y.T.2
  • 54
    • 67650498933 scopus 로고    scopus 로고
    • Ectodomain shedding and generation of two carboxy-terminal fragments of human complement receptor 2/CD21
    • M.M. Hoefer, and H. Illges Ectodomain shedding and generation of two carboxy-terminal fragments of human complement receptor 2/CD21 Mol. Immunol. 46 2009 2630 2639
    • (2009) Mol. Immunol. , vol.46 , pp. 2630-2639
    • Hoefer, M.M.1    Illges, H.2
  • 55
    • 65649127808 scopus 로고    scopus 로고
    • Soluble forms of RAGE in human diseases: Clinical and therapeutical implications
    • F. Santilli, N. Vazzana, L.G. Bucciarelli, and G. Davi Soluble forms of RAGE in human diseases: clinical and therapeutical implications Curr. Med. Chem. 16 2009 940 952
    • (2009) Curr. Med. Chem. , vol.16 , pp. 940-952
    • Santilli, F.1    Vazzana, N.2    Bucciarelli, L.G.3    Davi, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.