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Volumn 81, Issue 4, 2004, Pages 322-334

Evolutionary divergence of thyrotropin receptor structure

Author keywords

Evolution; Fish; Mammals; Rate shift analysis; TSH receptor

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; SERPENTINE; THYROTROPIN RECEPTOR;

EID: 1842523272     PISSN: 10967192     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ymgme.2004.01.010     Document Type: Article
Times cited : (8)

References (56)
  • 1
    • 0036083401 scopus 로고    scopus 로고
    • Thyroid-stimulating hormone and thyroid-stimulating hormone receptor structure-function relationships
    • Szkudlinski M.W., Fremont V., Ronin C., Weintraub B.D. Thyroid-stimulating hormone and thyroid-stimulating hormone receptor structure-function relationships. Physiol. Rev. 82:2001;473-502.
    • (2001) Physiol. Rev. , vol.82 , pp. 473-502
    • Szkudlinski, M.W.1    Fremont, V.2    Ronin, C.3    Weintraub, B.D.4
  • 2
    • 0034463310 scopus 로고    scopus 로고
    • Discovering new hormones, receptors and signalling mediators in the genomic era
    • Hsu S.Y., Hsueh A.J.W. Discovering new hormones, receptors and signalling mediators in the genomic era. Mol. Endocrinol. 14:2000;594-604.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 594-604
    • Hsu, S.Y.1    Hsueh, A.J.W.2
  • 3
    • 0036957787 scopus 로고    scopus 로고
    • The cysteine-rich C-flanking region of the thyrotropin receptor has very ancient phylogenetic origins: Implications from sequence analysis
    • Kaczur V., Racz I.A., Szendroi A., Takacs M., Farid N.R. The cysteine-rich C-flanking region of the thyrotropin receptor has very ancient phylogenetic origins: implications from sequence analysis. J. Endocr. Genet. 3:2002;46-54.
    • (2002) J. Endocr. Genet. , vol.3 , pp. 46-54
    • Kaczur, V.1    Racz, I.A.2    Szendroi, A.3    Takacs, M.4    Farid, N.R.5
  • 4
    • 0032247323 scopus 로고    scopus 로고
    • The thyrotropin (TSH)-releasing hormone receptor: Interaction with TSH and autoantibodies
    • Rapoport B., Chazenbalk G.D., Jaume J.C., McLachlan S.M. The thyrotropin (TSH)-releasing hormone receptor: interaction with TSH and autoantibodies. Endocr. Rev. 19:1998;673-716.
    • (1998) Endocr. Rev. , vol.19 , pp. 673-716
    • Rapoport, B.1    Chazenbalk, G.D.2    Jaume, J.C.3    McLachlan, S.M.4
  • 5
    • 0033910867 scopus 로고    scopus 로고
    • The human thyrotropin receptor is highly mutable: A review of gain-of-function mutations
    • Farid N.R., Kaczur V., Balazs C. The human thyrotropin receptor is highly mutable: a review of gain-of-function mutations. Eur. J. Endocrinol. 143:2000;25-30.
    • (2000) Eur. J. Endocrinol. , vol.143 , pp. 25-30
    • Farid, N.R.1    Kaczur, V.2    Balazs, C.3
  • 6
    • 1842561214 scopus 로고    scopus 로고
    • Available from http://www.gpcr.org.
  • 7
    • 0033803121 scopus 로고    scopus 로고
    • Identification of the sites of aspargine-linked glycosylation of the human thyrotropin receptor and studies on their role on receptor function and expression
    • Nagayama Y., Nishihara E., Namba H., Yamashita S., Niwa M. Identification of the sites of aspargine-linked glycosylation of the human thyrotropin receptor and studies on their role on receptor function and expression. J. Pharmacol. Exp. Ther. 2000;404-409.
    • (2000) J. Pharmacol. Exp. Ther. , pp. 404-409
    • Nagayama, Y.1    Nishihara, E.2    Namba, H.3    Yamashita, S.4    Niwa, M.5
  • 9
    • 0034793849 scopus 로고    scopus 로고
    • Regulation of thyroid cell proliferation by TSH and other factors: A critical evaluation of in vitro models
    • Kimura T., Van Keymeulen A., Golstein J., Fusco A., Dumont J.E., Roger P.P. Regulation of thyroid cell proliferation by TSH and other factors: a critical evaluation of in vitro models. Endocr. Rev. 22:2001;631-656.
    • (2001) Endocr. Rev. , vol.22 , pp. 631-656
    • Kimura, T.1    Van Keymeulen, A.2    Golstein, J.3    Fusco, A.4    Dumont, J.E.5    Roger, P.P.6
  • 10
    • 0027718173 scopus 로고
    • A structural basis of the interaction between leucine-rich repeats and protein ligands
    • Kobe B., Deisenhofer J. A structural basis of the interaction between leucine-rich repeats and protein ligands. Nature. 366:1993;751-756.
    • (1993) Nature , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 11
    • 0029645408 scopus 로고
    • Modelling of the three-dimensional structure of proteins with the typical leucine-rich repeats
    • Kajava A.V., Vassart G., Wodak S.J. Modelling of the three-dimensional structure of proteins with the typical leucine-rich repeats. Structure. 3:1995;867-877.
    • (1995) Structure , vol.3 , pp. 867-877
    • Kajava, A.V.1    Vassart, G.2    Wodak, S.J.3
  • 12
    • 0036218255 scopus 로고    scopus 로고
    • Lysine 183 and glutamic acid 157 of the TSH receptor: Two interacting residues with a key role in determining specificity towards TSH and human CG
    • Smits G., Govaerts C., Nubourgh I., Pardo L., Vassart G., Costagliola S. Lysine 183 and glutamic acid 157 of the TSH receptor: two interacting residues with a key role in determining specificity towards TSH and human CG. Endocrinology. 16:2002;722-735.
    • (2002) Endocrinology , vol.16 , pp. 722-735
    • Smits, G.1    Govaerts, C.2    Nubourgh, I.3    Pardo, L.4    Vassart, G.5    Costagliola, S.6
  • 13
    • 0030912536 scopus 로고    scopus 로고
    • A model of the lutropin/choriogonadotropin receptor: Insights into the structural and functional effects of constitutively activating mutations
    • Lin Z., Shenker A., Pearlstein R. A model of the lutropin/ choriogonadotropin receptor: insights into the structural and functional effects of constitutively activating mutations. Protein Eng. 10:1997;501-510.
    • (1997) Protein Eng. , vol.10 , pp. 501-510
    • Lin, Z.1    Shenker, A.2    Pearlstein, R.3
  • 19
    • 0034714979 scopus 로고    scopus 로고
    • Cloning and functional expression of a thyrotropin receptor from the gonads of a vertebrate (bony fish): Potential thyroid-dependent role for thyrotropin in reproduction
    • Kumar R.S., Ijiri S., Kight K., Swanson P., Dittman A., Alok D., Zoher Y., Trant J.M. Cloning and functional expression of a thyrotropin receptor from the gonads of a vertebrate (bony fish): potential thyroid-dependent role for thyrotropin in reproduction. Mol. Cell. Endocrinol. 167:2000;1-9.
    • (2000) Mol. Cell. Endocrinol. , vol.167 , pp. 1-9
    • Kumar, R.S.1    Ijiri, S.2    Kight, K.3    Swanson, P.4    Dittman, A.5    Alok, D.6    Zoher, Y.7    Trant, J.M.8
  • 21
    • 0035807886 scopus 로고    scopus 로고
    • A likelihood ratio test for evolutionary rate shifts and functional divergence among proteins
    • Knudsen B., Miyamoto M.M. A likelihood ratio test for evolutionary rate shifts and functional divergence among proteins. Proc. Natl. Acad. Sci. USA. 98:2001;14512-14517.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14512-14517
    • Knudsen, B.1    Miyamoto, M.M.2
  • 22
    • 0041817651 scopus 로고    scopus 로고
    • Using evolutionary rates to investigate protein functional divergence and conservation: A case study of the carbonic anhydrases
    • Knudsen B., Miyamoto M.M., Liapis P.J., Silverman D.N. Using evolutionary rates to investigate protein functional divergence and conservation: a case study of the carbonic anhydrases. Genetics. 164:2003;1261-1269.
    • (2003) Genetics , vol.164 , pp. 1261-1269
    • Knudsen, B.1    Miyamoto, M.M.2    Liapis, P.J.3    Silverman, D.N.4
  • 23
    • 0038363823 scopus 로고    scopus 로고
    • Cloning and functional characterization of a testicular TSH receptor cDNA from African catfish (Clarias garipinus)
    • Vischer H.F., Bogerd J. Cloning and functional characterization of a testicular TSH receptor cDNA from African catfish (Clarias garipinus). J. Mol. Endocrinol. 30:2003;227-238.
    • (2003) J. Mol. Endocrinol. , vol.30 , pp. 227-238
    • Vischer, H.F.1    Bogerd, J.2
  • 24
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive sequence alignment through sequence weighting, position specific gap penalties and matrix choices
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive sequence alignment through sequence weighting, position specific gap penalties and matrix choices. Nucleic Acids Res. 22:1994;4673-4780.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4780
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 25
    • 0030683599 scopus 로고    scopus 로고
    • PAML: A program package for phylogenetic analysis by maximum likelihood
    • Yang Z. PAML: a program package for phylogenetic analysis by maximum likelihood. Comput. Appl. Biosci. 13:1997;555-556.
    • (1997) Comput. Appl. Biosci. , vol.13 , pp. 555-556
    • Yang, Z.1
  • 26
  • 27
    • 0003728605 scopus 로고
    • Fishes of the World
    • New York, NY: John Wiley & Sons
    • Nelson J.S. Fishes of the World. third ed. 1994;John Wiley & Sons, New York, NY.
    • (1994) Third Ed.
    • Nelson, J.S.1
  • 28
    • 0035793620 scopus 로고    scopus 로고
    • Hormone interactions to the Leu-rich repeats in gonadotropin receptors. I. Analysis of Leu-rich repeats of human luteinizing hormone/chorionic gonadotropin receptor and follicule stimulating hormone receptor
    • Song Y.S., Ji I., Beauchamp J., Isaacs N.W., Ji T.H. Hormone interactions to the Leu-rich repeats in gonadotropin receptors. I. Analysis of Leu-rich repeats of human luteinizing hormone/chorionic gonadotropin receptor and follicule stimulating hormone receptor. J. Biol. Chem. 276:2001;3426-3435.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3426-3435
    • Song, Y.S.1    Ji, I.2    Beauchamp, J.3    Isaacs, N.W.4    Ji, T.H.5
  • 29
    • 0035793641 scopus 로고    scopus 로고
    • Hormone interactions to the Leu-rich repeats in gonadotropin receptors. II. Analysis of Leu-rich repeat 4 of human lutenizing hormone/chorionic gonadotropin receptor
    • Song Y.S., Ji I., Beauchamp J., Isaacs N.W., Ji T.H. Hormone interactions to the Leu-rich repeats in gonadotropin receptors. II. Analysis of Leu-rich repeat 4 of human lutenizing hormone/chorionic gonadotropin receptor. J. Biol. Chem. 276:2001;3436-3442.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3436-3442
    • Song, Y.S.1    Ji, I.2    Beauchamp, J.3    Isaacs, N.W.4    Ji, T.H.5
  • 30
    • 0035793633 scopus 로고    scopus 로고
    • Hormone interactions to the Leu-rich repeats in gonadotropin receptors. III. Photoaffinity cross-linking of the human chorionic gonadotropin with receptor Leu-rich repeat 4 peptide
    • Jeoung M., Phang T., Song Y.S., Ji I., Ji T.H. Hormone interactions to the Leu-rich repeats in gonadotropin receptors. III. Photoaffinity cross-linking of the human chorionic gonadotropin with receptor Leu-rich repeat 4 peptide. J. Biol. Chem. 276:2001;3443-3450.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3443-3450
    • Jeoung, M.1    Phang, T.2    Song, Y.S.3    Ji, I.4    Ji, T.H.5
  • 32
    • 0038182536 scopus 로고    scopus 로고
    • The role of the β-strands of extracellular leucine rich repeats 3 and 6 of the human luteinizing hormone receptor
    • Vischer H.F., Grannemen J.C.M., Noordam M.J., Mosselman S., Bogerd J. The role of the β-strands of extracellular leucine rich repeats 3 and 6 of the human luteinizing hormone receptor. J. Biol. Chem. 278:2003;15505-15513.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15505-15513
    • Vischer, H.F.1    Grannemen, J.C.M.2    Noordam, M.J.3    Mosselman, S.4    Bogerd, J.5
  • 33
    • 0142056956 scopus 로고    scopus 로고
    • Opposite contribution of two ligand-selective determinants in the N-terminal hormone-binding exodomain of human gonadotopin receptors
    • Vischer H.F., Granneman J.C.M., Bogerd J. Opposite contribution of two ligand-selective determinants in the N-terminal hormone-binding exodomain of human gonadotopin receptors. Mol. Endocrinol. 17:2003;1972-1981.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1972-1981
    • Vischer, H.F.1    Granneman, J.C.M.2    Bogerd, J.3
  • 34
    • 0036773467 scopus 로고    scopus 로고
    • Thyrotropin, follitropin, and chorionictropin expressed as a single multifunctional unit reveal remarkable permissiveness in receptor-ligand interactions
    • Garcia-Campayo V., Kumar T.R., Boime I. Thyrotropin, follitropin, and chorionictropin expressed as a single multifunctional unit reveal remarkable permissiveness in receptor-ligand interactions. Endocrinology. 143:2002;3773-3778.
    • (2002) Endocrinology , vol.143 , pp. 3773-3778
    • Garcia-Campayo, V.1    Kumar, T.R.2    Boime, I.3
  • 35
    • 0037225463 scopus 로고    scopus 로고
    • Specificity of cognate ligand receptor interactions: Fusion proteins of human chorionic gonadotropin and the heptahelical receptors for human lutenizing hormone, thyroid stimulating hormone, and follicule-stimulating hormone
    • Schubert R.L., Narayan P., Puett D. Specificity of cognate ligand receptor interactions: fusion proteins of human chorionic gonadotropin and the heptahelical receptors for human lutenizing hormone, thyroid stimulating hormone, and follicule-stimulating hormone. Endocrinology. 144:2003;129-137.
    • (2003) Endocrinology , vol.144 , pp. 129-137
    • Schubert, R.L.1    Narayan, P.2    Puett, D.3
  • 38
    • 0034730516 scopus 로고    scopus 로고
    • Activation of the lutenizing hormone receptor following substitution of Ser-277 with selective hydrophobic residues in the ectodomain hinge region
    • Nakabayashi K., Kudo M., Kobilka B., Hsueh A.J.W. Activation of the lutenizing hormone receptor following substitution of Ser-277 with selective hydrophobic residues in the ectodomain hinge region. J. Biol. Chem. 275:2000;30264-30271.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30264-30271
    • Nakabayashi, K.1    Kudo, M.2    Kobilka, B.3    Hsueh, A.J.W.4
  • 39
    • 0035793543 scopus 로고    scopus 로고
    • The role of the hinge region of the lutenizing hormone receptor in hormone interaction and signal generation
    • Zeng H., Phang T., Song Y.S., Ji I., Ji T.H. The role of the hinge region of the lutenizing hormone receptor in hormone interaction and signal generation. J. Biol. Chem. 276:2001;3451-3458.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3451-3458
    • Zeng, H.1    Phang, T.2    Song, Y.S.3    Ji, I.4    Ji, T.H.5
  • 40
    • 0042324612 scopus 로고    scopus 로고
    • Role of cleavage and shedding in human thyrotropin receptor function and trafficking
    • Quellari M., Desroches A., Beau I., Beaudeux E., Misrahi M. Role of cleavage and shedding in human thyrotropin receptor function and trafficking. Eur. J. Biochem. 270:2003;3486-3497.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3486-3497
    • Quellari, M.1    Desroches, A.2    Beau, I.3    Beaudeux, E.4    Misrahi, M.5
  • 41
    • 0034527615 scopus 로고    scopus 로고
    • A novel mutation in the thyrotropin (TSH) receptor causing loss of TSH binding but constitutive receptor activation in a family with resistance to TSH
    • Russo D., Betterie C., Arturi F., Chiefari E., Girelli M.E., Filletti S. A novel mutation in the thyrotropin (TSH) receptor causing loss of TSH binding but constitutive receptor activation in a family with resistance to TSH. J. Clin. Endocrinol. Metab. 85:2000;4238-4242.
    • (2000) J. Clin. Endocrinol. Metab. , vol.85 , pp. 4238-4242
    • Russo, D.1    Betterie, C.2    Arturi, F.3    Chiefari, E.4    Girelli, M.E.5    Filletti, S.6
  • 42
    • 0033054119 scopus 로고    scopus 로고
    • Characterization of a region of the lutropin recptor extracellular domain near transmembrane helix1 that is important in ligand-mediated signalling
    • Alveraz C.A., Narayan P., Huang J., Puett D. Characterization of a region of the lutropin recptor extracellular domain near transmembrane helix1 that is important in ligand-mediated signalling. Endocrinology. 140:1999;1775-1782.
    • (1999) Endocrinology , vol.140 , pp. 1775-1782
    • Alveraz, C.A.1    Narayan, P.2    Huang, J.3    Puett, D.4
  • 43
    • 0037634482 scopus 로고    scopus 로고
    • Structural analysis of yoked chorionic gonadotropin-lutenizing hormone receptor ectodomain complexes by circular dichroic spectroscopy
    • Fralish G.B., Dattilo B., Puett D. Structural analysis of yoked chorionic gonadotropin-lutenizing hormone receptor ectodomain complexes by circular dichroic spectroscopy. Mol. Endocrinol. 17:2003;1192-1202.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1192-1202
    • Fralish, G.B.1    Dattilo, B.2    Puett, D.3
  • 44
    • 0036214718 scopus 로고    scopus 로고
    • Activation of the cAMP pathway by the TSH receptor involves switching of the ectodomain from a tethered inverse agonist to an agonist
    • Vlaeminck-Guillem V., Ho S.-C., Rodien P., Vassart G., Costagliola S. Activation of the cAMP pathway by the TSH receptor involves switching of the ectodomain from a tethered inverse agonist to an agonist. Mol. Endocrinol. 16:2002;736-746.
    • (2002) Mol. Endocrinol. , vol.16 , pp. 736-746
    • Vlaeminck-Guillem, V.1    Ho, S.-C.2    Rodien, P.3    Vassart, G.4    Costagliola, S.5
  • 45
    • 0034987731 scopus 로고    scopus 로고
    • Effects of mutations involving the highly conserved S281 HCG motif in the extracellular domain of the thyrotropin (TSH) receptor in TSH binding and constitutive activity
    • Ho S.C., Van Sande J., Lefort A., Vassart G., Costagliola S. Effects of mutations involving the highly conserved S281 HCG motif in the extracellular domain of the thyrotropin (TSH) receptor in TSH binding and constitutive activity. Endocrinology. 142:2001;2760-2767.
    • (2001) Endocrinology , vol.142 , pp. 2760-2767
    • Ho, S.C.1    Van Sande, J.2    Lefort, A.3    Vassart, G.4    Costagliola, S.5
  • 47
    • 0035976910 scopus 로고    scopus 로고
    • Oligomerization of the human thyrotropin receptor: Fluorescent protein-tagged hTSHR reveals post-translational complexes
    • Latif R., Graves P., Davies T.F. Oligomerization of the human thyrotropin receptor: fluorescent protein-tagged hTSHR reveals post-translational complexes. J. Biol. Chem. 276:2001;45217-45224.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45217-45224
    • Latif, R.1    Graves, P.2    Davies, T.F.3
  • 48
    • 0021955069 scopus 로고
    • Structure of the porcine thyrotropin receptor: A 200 kDa glycoprotein heterocomplex
    • Islam M.N., Farid N.R. Structure of the porcine thyrotropin receptor: a 200. kDa glycoprotein heterocomplex Experientia. 41:1985;18-23.
    • (1985) Experientia , vol.41 , pp. 18-23
    • Islam, M.N.1    Farid, N.R.2
  • 49
    • 0035498937 scopus 로고    scopus 로고
    • Receptor activation: What does the rhodopsin structure tell us?
    • Meng E.C., Bourne H.R. Receptor activation: what does the rhodopsin structure tell us? Trends Phamacol. Sci. 22:2001;587-593.
    • (2001) Trends Phamacol. Sci. , vol.22 , pp. 587-593
    • Meng, E.C.1    Bourne, H.R.2
  • 50
    • 0343932883 scopus 로고
    • Exhibition of TSH-induced desensitisation in TSH receptor transfected CHO cells: Truncation of TSH receptor cytoplasmic tail does not affect homologous desensitisation
    • Shi Y., Zou M., Ahring P., Farid N.R. Exhibition of TSH-induced desensitisation in TSH receptor transfected CHO cells: truncation of TSH receptor cytoplasmic tail does not affect homologous desensitisation. Endocr. J. 1:1993;157-162.
    • (1993) Endocr. J. , vol.1 , pp. 157-162
    • Shi, Y.1    Zou, M.2    Ahring, P.3    Farid, N.R.4
  • 53
    • 0141447331 scopus 로고    scopus 로고
    • Proper targeting and activity of a non-functioning thyroid-stimulating hormone receptor (TSHr) combining an inactivating and activating TSHr mutation in one receptor
    • Argetti P., de Marco G., Collecchi P., Chiovato L., Vitti P., Pinchera A., Tonacchera M. Proper targeting and activity of a non-functioning thyroid-stimulating hormone receptor (TSHr) combining an inactivating and activating TSHr mutation in one receptor. Eur. J. Biochem. 270:2003;3839-3847.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3839-3847
    • Argetti, P.1    De Marco, G.2    Collecchi, P.3    Chiovato, L.4    Vitti, P.5    Pinchera, A.6    Tonacchera, M.7
  • 54


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