메뉴 건너뛰기




Volumn 12, Issue 14, 1998, Pages 1461-1471

A conserved tyrosine residue (Y601) in transmembrane domain 5 of the human thyrotropin receptor serves as a molecular switch to determine G- protein coupling

Author keywords

G protein coupled receptor; Molecular modeling; Receptor conformation; Thyroid; TSH receptor allele

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; THYROTROPIN RECEPTOR; TYROSINE;

EID: 0031790855     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.12.14.1461     Document Type: Article
Times cited : (83)

References (53)
  • 1
    • 0026743033 scopus 로고
    • The thyrotropin receptor and the regulation of thyrocyte function and growth
    • Vassart, G., and Dumont, J. E. (1992) The thyrotropin receptor and the regulation of thyrocyte function and growth. Endocr. Rev. 13, 596-611
    • (1992) Endocr. Rev. , vol.13 , pp. 596-611
    • Vassart, G.1    Dumont, J.E.2
  • 2
    • 0026568620 scopus 로고
    • The thyrotropin receptor 25 years after its discovery: New insight after its molecular cloning
    • Nagayama, Y., and Rapoport, B. (1992) The thyrotropin receptor 25 years after its discovery: new insight after its molecular cloning. Mol. Endocrinol. 6, 145-156
    • (1992) Mol. Endocrinol. , vol.6 , pp. 145-156
    • Nagayama, Y.1    Rapoport, B.2
  • 3
    • 0028909714 scopus 로고
    • Receptors and G proteins as primary components of transmembrane signal transduction, Part 1. G-protein-coupled receptors: Structure and function
    • Gudermann, T., Nürnberg, B., and Schultz, G. (1995) Receptors and G proteins as primary components of transmembrane signal transduction, Part 1. G-protein-coupled receptors: structure and function. J. Mol. Med. 73, 51-63
    • (1995) J. Mol. Med. , vol.73 , pp. 51-63
    • Gudermann, T.1    Nürnberg, B.2    Schultz, G.3
  • 4
    • 0025237466 scopus 로고
    • The testicular receptor for follicle stimulating hormone: Structure and functional expression of cloned cDNA
    • Sprengel, R., Braun, T., Nikulics., K., Segaloff, D. L., and Seeburg, P. H. (1990) The testicular receptor for follicle stimulating hormone: structure and functional expression of cloned cDNA. Mol. Endocrinol. 4, 525-530
    • (1990) Mol. Endocrinol. , vol.4 , pp. 525-530
    • Sprengel, R.1    Braun, T.2    Nikulics, K.3    Segaloff, D.L.4    Seeburg, P.H.5
  • 5
    • 0027158153 scopus 로고
    • The lutropin/ choriogonadotropin receptor. . . 4 years later
    • Segaloff, D. L., and Ascoli, M. (1993) The lutropin/ choriogonadotropin receptor. . . 4 years later. Endocr. Rev. 14, 324-347
    • (1993) Endocr. Rev. , vol.14 , pp. 324-347
    • Segaloff, D.L.1    Ascoli, M.2
  • 8
    • 0028863032 scopus 로고
    • TSH receptor and LH receptor
    • Kosugi, S., and Mori, T. (1995) TSH receptor and LH receptor. Endocr. J. 42,587-606
    • (1995) Endocr. J. , vol.42 , pp. 587-606
    • Kosugi, S.1    Mori, T.2
  • 11
    • 0024852495 scopus 로고
    • Molecular cloning, sequence and functional expression of the cDNA for the human thyrotropin receptor
    • Nagayama, Y., Kaufman, K. D., Seto, P., and Rapoport, B. (1989) Molecular cloning, sequence and functional expression of the cDNA for the human thyrotropin receptor. Biochem. Biophys. Res. Commun. 165, 1184-1190
    • (1989) Biochem. Biophys. Res. Commun. , vol.165 , pp. 1184-1190
    • Nagayama, Y.1    Kaufman, K.D.2    Seto, P.3    Rapoport, B.4
  • 15
    • 85016731055 scopus 로고
    • Using PCR to engineer DNA
    • Ehrlich, H. A., ed, Stockton Press, New York
    • Higuchi, R. (1989) Using PCR to engineer DNA. In PCR Technology (Ehrlich, H. A., ed) pp 61-70, Stockton Press, New York
    • (1989) PCR Technology , pp. 61-70
    • Higuchi, R.1
  • 16
    • 0030983833 scopus 로고    scopus 로고
    • Mutations of the human thyrotropin receptor gene causing thyroid hypoplasia and persistent congenital hypothyroidism
    • Biebermann, H., Schöneberg, T., Krude, H., Schultz, G., Gudermann, T., and Grüters, A. (1997) Mutations of the human thyrotropin receptor gene causing thyroid hypoplasia and persistent congenital hypothyroidism. J. Clin. Endocrinol. Metah. 82, 3471-3480
    • (1997) J. Clin. Endocrinol. Metah. , vol.82 , pp. 3471-3480
    • Biebermann, H.1    Schöneberg, T.2    Krude, H.3    Schultz, G.4    Gudermann, T.5    Grüters, A.6
  • 17
    • 77957042700 scopus 로고
    • Techniques for human adenovirus vector construction and characterization
    • Adolph, K. W., ed, Academic Press, San Diego
    • Hitt, M., Bett, A. J., Addison, C. L., Prevec, L., and Graham, F. L. (1995) Techniques for human adenovirus vector construction and characterization. In Viral Gene Techniques (Adolph, K. W., ed) pp 13-30, Academic Press, San Diego
    • (1995) Viral Gene Techniques , pp. 13-30
    • Hitt, M.1    Bett, A.J.2    Addison, C.L.3    Prevec, L.4    Graham, F.L.5
  • 18
    • 0029077235 scopus 로고
    • Plasma membrane localization and functional rescue of truncated forms of a G protein-coupled receptor
    • Schöneberg, T., Liu, J., and Wess, J. (1995) Plasma membrane localization and functional rescue of truncated forms of a G protein-coupled receptor. J. Biol. Chem. 270, 18000-18006
    • (1995) J. Biol. Chem. , vol.270 , pp. 18000-18006
    • Schöneberg, T.1    Liu, J.2    Wess, J.3
  • 19
    • 0030006129 scopus 로고    scopus 로고
    • Functional rescue of mutant V2 vasopressin receptors causing nephrogenic diabetes insipidus by a co-expressed receptor polypeptide
    • Schöneberg, T., Yun, J., Wenkert, D., and Wess, J. (1996) Functional rescue of mutant V2 vasopressin receptors causing nephrogenic diabetes insipidus by a co-expressed receptor polypeptide. EMBO J. 15, 1283-1291
    • (1996) EMBO J. , vol.15 , pp. 1283-1291
    • Schöneberg, T.1    Yun, J.2    Wenkert, D.3    Wess, J.4
  • 22
    • 3643079429 scopus 로고
    • G-protein coupled receptors, glucagon type: How to overcome the alignment/fit dilemma to the bacteriorhodopsin template
    • Sanz, F., ed, Prous Science Publishers, Barcelona
    • Krause, G., Kühne, R., and Rubel, S. (1995) G-protein coupled receptors, glucagon type: How to overcome the alignment/fit dilemma to the bacteriorhodopsin template. In QSAR and Molecular Modelling: Concepts, Computational Tools and Applications (Sanz, F., ed) pp 530-533, Prous Science Publishers, Barcelona
    • (1995) QSAR and Molecular Modelling: Concepts, Computational Tools and Applications , pp. 530-533
    • Krause, G.1    Kühne, R.2    Rubel, S.3
  • 23
    • 0029845242 scopus 로고    scopus 로고
    • A database of mutants and effects of site-directed mutagenesis experiments on G protein-coupled receptors
    • Kristiansen, K., Dahl, S. G., and Edvardson, O. (1996) A database of mutants and effects of site-directed mutagenesis experiments on G protein-coupled receptors. Proteins 26, 1-94
    • (1996) Proteins , vol.26 , pp. 1-94
    • Kristiansen, K.1    Dahl, S.G.2    Edvardson, O.3
  • 24
    • 0031565726 scopus 로고    scopus 로고
    • An α-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • Baldwin, J. M., Schertler, G. F. X., and Unger, V. M. (1997) An α-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors. J. Mol. Biol, 272, 144-164
    • (1997) J. Mol. Biol , vol.272 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.X.2    Unger, V.M.3
  • 25
    • 84988053694 scopus 로고
    • An all atom forcefield for simulation of proteins and nucleic acids
    • Weiner, S. J., Kollmann, P. A., Nguyen, D. T., and Case, D. A. (1986) An all atom forcefield for simulation of proteins and nucleic acids. J. Comp. Chem. 7, 230-252
    • (1986) J. Comp. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollmann, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 26
    • 0030841110 scopus 로고    scopus 로고
    • Three dimensional structure of the cytoplasmic face of the G-protein receptor rhodopsin
    • Yeagle, P. L., Alderfer, J. L., and Albert, A. D. (1997) Three dimensional structure of the cytoplasmic face of the G-protein receptor rhodopsin. Biochemistry 36, 9649-9654
    • (1997) Biochemistry , vol.36 , pp. 9649-9654
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 27
    • 0026666278 scopus 로고
    • 2+ mobilization. Studies with the cloned murine luteinizing hormone receptor expressed in L cells
    • 2+ mobilization. Studies with the cloned murine luteinizing hormone receptor expressed in L cells. J. Biol. Chem. 267, 4479-4488
    • (1992) J. Biol. Chem. , vol.267 , pp. 4479-4488
    • Gudermann, T.1    Birnbaumer, M.2    Birnbaumer, L.3
  • 28
    • 0028244065 scopus 로고
    • Functional role of a cytoplasmic aromatic amino acid in muscarinic receptor-mediated activation of phospholipase C
    • Blüml, K., Mutschler, E., and Wess, J. (1994) Functional role of a cytoplasmic aromatic amino acid in muscarinic receptor-mediated activation of phospholipase C.J. Biol. Chem. 269, 11537-11541
    • (1994) J. Biol. Chem. , vol.269 , pp. 11537-11541
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 29
    • 0028158607 scopus 로고
    • Identification of an intracellular tyrosine residue for muscarinic receptor-mediated stimulation of phosphatidyl inositol hydrolysis
    • Blüml, K., Mutschler, E., and Wess, J. (1994) Identification of an intracellular tyrosine residue for muscarinic receptor-mediated stimulation of phosphatidyl inositol hydrolysis. J. Biol. Chem. 269, 402-405
    • (1994) J. Biol. Chem. , vol.269 , pp. 402-405
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 30
    • 0030068064 scopus 로고    scopus 로고
    • Differential effects of NaCl concentration on the constitutive activity of the thyrotropin and the luteinizing hormone/chorionic gonadotropin receptors
    • Cetani, F., Tonacchera, M., and Vassart, G. (1996) Differential effects of NaCl concentration on the constitutive activity of the thyrotropin and the luteinizing hormone/chorionic gonadotropin receptors. FEBS Lett. 378, 27-31
    • (1996) FEBS Lett. , vol.378 , pp. 27-31
    • Cetani, F.1    Tonacchera, M.2    Vassart, G.3
  • 31
    • 0029907599 scopus 로고    scopus 로고
    • Requirements of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens, D. L., Altenbach, C., Yang, K., Hubbell, W. L., and Khorana, H. G. (1996) Requirements of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274, 768-770
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 34
    • 0029778268 scopus 로고    scopus 로고
    • Rhoriopsin activation blocked by metalion-binding sites linking transmembrane helices C and F
    • Sheikh, S. P., Zvyaga, T. A., Lichtarge, O., Sakmar, T. P., and Bourne, H. R. (1996) Rhoriopsin activation blocked by metalion-binding sites linking transmembrane helices C and F. Nature (London) 383, 347-350
    • (1996) Nature (London) , vol.383 , pp. 347-350
    • Sheikh, S.P.1    Zvyaga, T.A.2    Lichtarge, O.3    Sakmar, T.P.4    Bourne, H.R.5
  • 35
    • 0030859541 scopus 로고    scopus 로고
    • Agonist induce conformational changes in transmembrane domains III and VI of the ß2 adrenoreceptor
    • Gether, U., Lin, S., Ghanouni, P., Ballesteros, J. A., Weinstein, H., and Kobilka, B. K. (1997) Agonist induce conformational changes in transmembrane domains III and VI of the ß2 adrenoreceptor. EMBO J. 16, 6737-6747
    • (1997) EMBO J. , vol.16 , pp. 6737-6747
    • Gether, U.1    Lin, S.2    Ghanouni, P.3    Ballesteros, J.A.4    Weinstein, H.5    Kobilka, B.K.6
  • 36
    • 0028888593 scopus 로고
    • Brief report: Resistance to thyrotropin caused by mutations in the thyrotropin-receptorgene
    • Sunthornthepvarakul, T., Gottschalk, M. E., Hayashi, Y., and Retetoff, S. (1995) Brief report: resistance to thyrotropin caused by mutations in the thyrotropin-receptorgene. N. Engl. J. Med. 332, 155-160
    • (1995) N. Engl. J. Med. , vol.332 , pp. 155-160
    • Sunthornthepvarakul, T.1    Gottschalk, M.E.2    Hayashi, Y.3    Retetoff, S.4
  • 39
    • 0030901754 scopus 로고    scopus 로고
    • Congenital hypothyroidism caused by mutations in the thyrotropin-receptor gene
    • Biebermann, H., Grüters, A., Schöneberg, T., and Gudermann, T. (1997) Congenital hypothyroidism caused by mutations in the thyrotropin-receptor gene. N. Engl. J. Med. 336, 1390-1391
    • (1997) N. Engl. J. Med. , vol.336 , pp. 1390-1391
    • Biebermann, H.1    Grüters, A.2    Schöneberg, T.3    Gudermann, T.4
  • 40
    • 0030994365 scopus 로고    scopus 로고
    • Familial congenital hypothyroidism due to inactivating mutation of the thyrotropin receptor causing profound hypoplasia of the thyroid gland
    • Abramowicz, M. J., Duprez, L., Parma, J., Vassart, G., and Heinrichs, C. (1997) Familial congenital hypothyroidism due to inactivating mutation of the thyrotropin receptor causing profound hypoplasia of the thyroid gland. J. Clin. Invest. 99, 3018-3024
    • (1997) J. Clin. Invest. , vol.99 , pp. 3018-3024
    • Abramowicz, M.J.1    Duprez, L.2    Parma, J.3    Vassart, G.4    Heinrichs, C.5
  • 41
    • 0028962470 scopus 로고
    • Critical role of a conserved intramembrane tyrosine residue in angiotensin II receptor activation
    • Hunyady, L., Bor, M., Balla, T., and Catt, K. J. (1995) Critical role of a conserved intramembrane tyrosine residue in angiotensin II receptor activation. J. Biol. Chem. 270, 9702-9705
    • (1995) J. Biol. Chem. , vol.270 , pp. 9702-9705
    • Hunyady, L.1    Bor, M.2    Balla, T.3    Catt, K.J.4
  • 43
    • 0029964709 scopus 로고    scopus 로고
    • Identification of amino acid residues in transmembrane helices VI and VII of the lutropin/choriogonadotropin receptor involved in signaling
    • Fernandez, L. M., and Puett, D. (1996) Identification of amino acid residues in transmembrane helices VI and VII of the lutropin/choriogonadotropin receptor involved in signaling. Biochemistry 35,3986-3993
    • (1996) Biochemistry , vol.35 , pp. 3986-3993
    • Fernandez, L.M.1    Puett, D.2
  • 44
    • 0029670790 scopus 로고
    • Lys583 in the third extracellular loop of the lutropin/choriogonadotropin receptor is critical for signaling
    • Fernandez, L. M., and Puett, D. (1990) Lys583 in the third extracellular loop of the lutropin/choriogonadotropin receptor is critical for signaling. J. Biol. Chem. 271, 925-930
    • (1990) J. Biol. Chem. , vol.271 , pp. 925-930
    • Fernandez, L.M.1    Puett, D.2
  • 45
    • 0030912536 scopus 로고    scopus 로고
    • A model of lutropin/choriogonadotropin receptor; insights into the structural and functional effects of constitutively activating mutations
    • Lin, Z, Shenker, A., and Perlstein, R. (1997) A model of lutropin/choriogonadotropin receptor; insights into the structural and functional effects of constitutively activating mutations. Protein Engin. 10, 501-510
    • (1997) Protein Engin. , vol.10 , pp. 501-510
    • Lin, Z.1    Shenker, A.2    Perlstein, R.3
  • 47
    • 0027297275 scopus 로고
    • Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins
    • Lefkowitz, R. J., Cotecchia, S., Samama, P., and Costa, T. (1993) Constitutive activity of receptors coupled to guanine nucleotide regulatory proteins. Trends Pharmacol. Sci. 14, 303-307
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 303-307
    • Lefkowitz, R.J.1    Cotecchia, S.2    Samama, P.3    Costa, T.4
  • 49
    • 0026592357 scopus 로고
    • Constitutive activation of the am-adrenergic receptor by all amino acid substitution at a single site. Evidence for a region which constrains receptor activation
    • Kjelsberg, M. A., Cotecchia, S., Ostrowski, J., Caron, M. G., and Lefkowitz, R. J. (1992) Constitutive activation of the am-adrenergic receptor by all amino acid substitution at a single site. Evidence for a region which constrains receptor activation. J. Biol. Chem. 267, 1430-1433
    • (1992) J. Biol. Chem. , vol.267 , pp. 1430-1433
    • Kjelsberg, M.A.1    Cotecchia, S.2    Ostrowski, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 51
    • 0029784196 scopus 로고    scopus 로고
    • The luteinizing hormone/chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals
    • Gilchrist, R. L., Ryu, K. S., Ji, I., and Ji, T. H. (1996) The luteinizing hormone/chorionic gonadotropin receptor has distinct transmembrane conductors for cAMP and inositol phosphate signals. J. Biol. Chem. 271, 19283-19287
    • (1996) J. Biol. Chem. , vol.271 , pp. 19283-19287
    • Gilchrist, R.L.1    Ryu, K.S.2    Ji, I.3    Ji, T.H.4
  • 52
    • 0030939070 scopus 로고    scopus 로고
    • Induction of promiscuous G protein coupling of the follicle-stimulating hormone (FSH) receptor: A novel mechanism for transducing pleiotropic actions of FSH isoforms
    • Arey, B. J., Stevis, P. E., Deecher, D. C., Shen, E. S., Frail, D. E., Negro-Vilar, A., and Lopez, F.J. (1997) Induction of promiscuous G protein coupling of the follicle-stimulating hormone (FSH) receptor: a novel mechanism for transducing pleiotropic actions of FSH isoforms. Mol. Endocrinol. 11, 517-526
    • (1997) Mol. Endocrinol. , vol.11 , pp. 517-526
    • Arey, B.J.1    Stevis, P.E.2    Deecher, D.C.3    Shen, E.S.4    Frail, D.E.5    Negro-Vilar, A.6    Lopez, F.J.7
  • 53
    • 0030013815 scopus 로고    scopus 로고
    • Site-directedmutagenesis of amino acids 33-44 of the common alpha-subunit reveals different structural requirements for heterodimer expression among the glycoprotein hormones and suggests that cyclic adenosine 3',5'-monophosphate production and growth promotion are potentially dissociable functions of human thyrotropin
    • Grossman, M., Szkudlinski, M. W., Dias, J. A., Xia, H., Wong, R., Puett, D., and Weintraub, B. D. (1996) Site-directedmutagenesis of amino acids 33-44 of the common alpha-subunit reveals different structural requirements for heterodimer expression among the glycoprotein hormones and suggests that cyclic adenosine 3',5'-monophosphate production and growth promotion are potentially dissociable functions of human thyrotropin. Mol. Endocrinol. 10, 769-777
    • (1996) Mol. Endocrinol. , vol.10 , pp. 769-777
    • Grossman, M.1    Szkudlinski, M.W.2    Dias, J.A.3    Xia, H.4    Wong, R.5    Puett, D.6    Weintraub, B.D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.