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Volumn 27, Issue 6, 2013, Pages 1004-1014

PRR repeats in the intracellular domain of KISS1R are important for its export to cell membrane

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR 54; INOSITOL PHOSPHATE; KISSPEPTIN; MITOGEN ACTIVATED PROTEIN KINASE; PROLINE;

EID: 84877909614     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2012-1386     Document Type: Article
Times cited : (17)

References (44)
  • 1
    • 0030698188 scopus 로고    scopus 로고
    • A family with hypogonadotropic hypogonadism and mutations in the gonadotropin-releasing hormone receptor
    • de Roux N, Young J, Misrahi M, et al. A family with hypogonadotropic hypogonadism and mutations in the gonadotropin-releasing hormone receptor. N Engl J Med. 1997;337:1597-1602.
    • (1997) N Engl J Med , vol.337 , pp. 1597-1602
    • de Roux, N.1    Young, J.2    Misrahi, M.3
  • 2
    • 67649390886 scopus 로고    scopus 로고
    • Isolated familial hypogonadotropic hypogonadism and a GNRH1 mutation
    • Bouligand J, Ghervan C, Tello JA, et al. Isolated familial hypogonadotropic hypogonadism and a GNRH1 mutation. N Engl J Med. 2009;360:2742-2748.
    • (2009) N Engl J Med , vol.360 , pp. 2742-2748
    • Bouligand, J.1    Ghervan, C.2    Tello, J.A.3
  • 3
    • 84857126496 scopus 로고    scopus 로고
    • Inactivating KISS1 mutation and hypogonadotropic hypogonadism
    • Topaloglu AK, Tello JA, Kotan LD, et al. Inactivating KISS1 mutation and hypogonadotropic hypogonadism. N Engl J Med. 2012; 366:629-635.
    • (2012) N Engl J Med , vol.366 , pp. 629-635
    • Topaloglu, A.K.1    Tello, J.A.2    Kotan, L.D.3
  • 4
    • 0141814637 scopus 로고    scopus 로고
    • Hypogonadotropic hypogonadism due to loss of function of the KiSS1-derived peptide receptor GPR54
    • de Roux N, Genin E, Carel JC, Matsuda F, Chaussain JL, Milgrom E. Hypogonadotropic hypogonadism due to loss of function of the KiSS1-derived peptide receptor GPR54. Proc Natl Acad Sci USA. 2003;100:10972-10976.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10972-10976
    • de Roux, N.1    Genin, E.2    Carel, J.C.3    Matsuda, F.4    Chaussain, J.L.5    Milgrom, E.6
  • 6
    • 61349091041 scopus 로고    scopus 로고
    • TAC3 and TACR3 mutations in familial hypogonadotropic hypogonadism reveal a key role for neurokinin B in the central control of reproduction
    • Topaloglu AK, Reimann F, Guclu M, et al. TAC3 and TACR3 mutations in familial hypogonadotropic hypogonadism reveal a key role for neurokinin B in the central control of reproduction. Nat Genet. 2009;41:354-358.
    • (2009) Nat Genet , vol.41 , pp. 354-358
    • Topaloglu, A.K.1    Reimann, F.2    Guclu, M.3
  • 7
    • 84455188563 scopus 로고    scopus 로고
    • Kisspeptin signaling is indispensable for neurokinin B, but not glutamate, stimulation of gonadotropin secretion in mice
    • García-Galiano D, van Ingen Schenau D, Leon S, et al. Kisspeptin signaling is indispensable for neurokinin B, but not glutamate, stimulation of gonadotropin secretion in mice. Endocrinology. 2012; 153:316-328.
    • (2012) Endocrinology , vol.153 , pp. 316-328
    • García-Galiano, D.1    van Ingen Schenau, D.2    Leon, S.3
  • 8
    • 35948986402 scopus 로고    scopus 로고
    • The role of kisspeptin- GPR54 signaling in the tonic regulation and surge release of gonadotropin- releasing hormone/luteinizing hormone
    • Dungan HM, Gottsch ML, Zeng H, et al. The role of kisspeptin- GPR54 signaling in the tonic regulation and surge release of gonadotropin- releasing hormone/luteinizing hormone. J Neurosci. 2007; 27:12088-12095.
    • (2007) J Neurosci , vol.27 , pp. 12088-12095
    • Dungan, H.M.1    Gottsch, M.L.2    Zeng, H.3
  • 10
    • 29644447614 scopus 로고    scopus 로고
    • Role of sequence variations of the GnRH receptor and G protein-coupled receptor 54 gene in male idiopathic hypogonadotropic hypogonadism
    • Lanfranco F, Gromoll J, von Eckardstein S, Herding EM, Nieschlag E, Simoni M. Role of sequence variations of the GnRH receptor and G protein-coupled receptor 54 gene in male idiopathic hypogonadotropic hypogonadism. Eur J Endocrinol. 2005;153:845-852.
    • (2005) Eur J Endocrinol , vol.153 , pp. 845-852
    • Lanfranco, F.1    Gromoll, J.2    von Eckardstein, S.3    Herding, E.M.4    Nieschlag, E.5    Simoni, M.6
  • 11
    • 79952307060 scopus 로고    scopus 로고
    • A novel loss-of-function mutation in GPR54/KISS1R leads to hypogonadotropic hypogonadism in a highly consanguineous family
    • Nimri R, Lebenthal Y, Lazar L, et al. A novel loss-of-function mutation in GPR54/KISS1R leads to hypogonadotropic hypogonadism in a highly consanguineous family. J Clin Endocrinol Metab. 2011;96:E536-E545.
    • (2011) J Clin Endocrinol Metab , vol.96
    • Nimri, R.1    Lebenthal, Y.2    Lazar, L.3
  • 12
    • 15944368215 scopus 로고    scopus 로고
    • Two novel missense mutations in g protein-coupled receptor 54 in a patient with hypogonadotropic hypogonadism
    • Semple RK, Achermann JC, Ellery J, et al. Two novel missense mutations in g protein-coupled receptor 54 in a patient with hypogonadotropic hypogonadism. J Clin Endocrinol Metab. 2005; 90:1849-1855.
    • (2005) J Clin Endocrinol Metab , vol.90 , pp. 1849-1855
    • Semple, R.K.1    Achermann, J.C.2    Ellery, J.3
  • 13
    • 77954112496 scopus 로고    scopus 로고
    • A novel homozygous splice acceptor site mutation of KISS1R in two siblings with normosmic isolated hypogonadotropic hypogonadism
    • Teles MG, Trarbach EB, Noel SD, et al. A novel homozygous splice acceptor site mutation of KISS1R in two siblings with normosmic isolated hypogonadotropic hypogonadism. Eur J Endocrinol. 2010;163:29-34.
    • (2010) Eur J Endocrinol , vol.163 , pp. 29-34
    • Teles, M.G.1    Trarbach, E.B.2    Noel, S.D.3
  • 14
    • 33947493910 scopus 로고    scopus 로고
    • Neuroendocrine phenotype analysis in five patients with isolated hypogonadotropic hypogonadism due to a L102P inactivating mutation of GPR54
    • Tenenbaum-Rakover Y, Commenges-Ducos M, Iovane A, Aumas C, Admoni O, de Roux N. Neuroendocrine phenotype analysis in five patients with isolated hypogonadotropic hypogonadism due to a L102P inactivating mutation of GPR54. J Clin Endocrinol Metab. 2007;92:1137-1144.
    • (2007) J Clin Endocrinol Metab , vol.92 , pp. 1137-1144
    • Tenenbaum-Rakover, Y.1    Commenges-Ducos, M.2    Iovane, A.3    Aumas, C.4    Admoni, O.5    de Roux, N.6
  • 15
    • 84864371825 scopus 로고    scopus 로고
    • A novel severe N-terminal splice site KISS1R gene mutation causes hypogonadotropic hypogonadism but enables a normal development of neonatal external genitalia
    • Breuer O, Abdulhadi-Atwan M, Zeligson S, et al. A novel severe N-terminal splice site KISS1R gene mutation causes hypogonadotropic hypogonadism but enables a normal development of neonatal external genitalia. Eur J Endocrinol. 2012;167:209-216.
    • (2012) Eur J Endocrinol , vol.167 , pp. 209-216
    • Breuer, O.1    Abdulhadi-Atwan, M.2    Zeligson, S.3
  • 16
    • 34547533091 scopus 로고    scopus 로고
    • Hypogonadotropic hypogonadism in mice lacking a functional Kiss1 gene
    • d'Anglemont de Tassigny X, Fagg LA, et al. Hypogonadotropic hypogonadism in mice lacking a functional Kiss1 gene. Proc Natl Acad Sci USA. 2007;104:10714-10719.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 10714-10719
    • d'Anglemont de Tassigny, X.1    Fagg, L.A.2
  • 17
    • 34748900269 scopus 로고    scopus 로고
    • Kiss1-/- mice exhibit more variable hypogonadism than Gpr54-/- mice
    • Lapatto R, Pallais JC, Zhang D, et al. Kiss1-/- mice exhibit more variable hypogonadism than Gpr54-/- mice. Endocrinology. 2007;148:4927-4936.
    • (2007) Endocrinology , vol.148 , pp. 4927-4936
    • Lapatto, R.1    Pallais, J.C.2    Zhang, D.3
  • 18
    • 77957001039 scopus 로고    scopus 로고
    • Oligogenic basis of isolated gonadotropin-releasing hormone deficiency
    • Sykiotis GP, Plummer L, Hughes VA, et al. Oligogenic basis of isolated gonadotropin-releasing hormone deficiency. Proc Natl Acad Sci USA. 2010;107:15140-15144.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 15140-15144
    • Sykiotis, G.P.1    Plummer, L.2    Hughes, V.A.3
  • 19
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics. 2008;9:40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 21
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theor Comp. 2008;4:435-447.
    • (2008) J Chem Theor Comp , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 22
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 23
    • 0034669774 scopus 로고    scopus 로고
    • Bayesian probabilistic approach for predicting backbone structures in terms of protein blocks
    • de Brevern AG, Etchebest C, Hazout S. Bayesian probabilistic approach for predicting backbone structures in terms of protein blocks. Proteins. 2000;41:271-287.
    • (2000) Proteins , vol.41 , pp. 271-287
    • de Brevern, A.G.1    Etchebest, C.2    Hazout, S.3
  • 25
    • 33747877568 scopus 로고    scopus 로고
    • Ontogeny and mechanisms of action for the stimulatory effect of kisspeptin on gonadotropin-releasing hormone system of the rat
    • Castellano JM, Navarro VM, Fernandez-Fernandez R, et al. Ontogeny and mechanisms of action for the stimulatory effect of kisspeptin on gonadotropin-releasing hormone system of the rat. Mol Cell Endocrinol. 2006;257-258:75-83.
    • (2006) Mol Cell Endocrinol , vol.257-258 , pp. 75-83
    • Castellano, J.M.1    Navarro, V.M.2    Fernandez-Fernandez, R.3
  • 26
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schäffer AA, et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997;25:3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schäffer, A.A.3
  • 28
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position- specific scoring matrices
    • Jones DT. Protein secondary structure prediction based on position- specific scoring matrices. J Mol Biol. 1999;292:195-202.
    • (1999) J Mol Biol , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 29
    • 79551504959 scopus 로고    scopus 로고
    • Predicting protein flexibility through the prediction of local structures
    • Bornot A, Etchebest C, de Brevern AG. Predicting protein flexibility through the prediction of local structures. Proteins. 2011;79:839-852.
    • (2011) Proteins , vol.79 , pp. 839-852
    • Bornot, A.1    Etchebest, C.2    de Brevern, A.G.3
  • 30
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, Zhang Y. I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc. 2010;5:725-738.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 31
    • 0028097921 scopus 로고
    • The structure and function of proline-rich regions in proteins
    • Williamson MP. The structure and function of proline-rich regions in proteins. Biochem J. 1994;297:249-260.
    • (1994) Biochem J , vol.297 , pp. 249-260
    • Williamson, M.P.1
  • 32
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol. 1993;234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 34
    • 33746527488 scopus 로고    scopus 로고
    • Inactivating mutations ofGprotein-coupled receptors and diseases: Structure-function insights and therapeutic implications
    • Tao YX. Inactivating mutations ofGprotein-coupled receptors and diseases: structure-function insights and therapeutic implications. Pharmacol Ther. 2006;111:949-973.
    • (2006) Pharmacol Ther , vol.111 , pp. 949-973
    • Tao, Y.X.1
  • 35
    • 79957562543 scopus 로고    scopus 로고
    • G protein-coupled receptors: Mutations and endocrine diseases
    • Vassart G, Costagliola S. G protein-coupled receptors: mutations and endocrine diseases. Nat Rev Endocrinol. 2011;7:362-372.
    • (2011) Nat Rev Endocrinol , vol.7 , pp. 362-372
    • Vassart, G.1    Costagliola, S.2
  • 36
    • 0029003359 scopus 로고
    • Ontogeny of gonadotropin, testosterone, and inhibin secretion in normal boys through puberty based on overnight serial sampling
    • Manasco PK, Umbach DM, Muly SM, et al. Ontogeny of gonadotropin, testosterone, and inhibin secretion in normal boys through puberty based on overnight serial sampling. J Clin Endocrinol Metab. 1995;80:2046-2052.
    • (1995) J Clin Endocrinol Metab , vol.80 , pp. 2046-2052
    • Manasco, P.K.1    Umbach, D.M.2    Muly, S.M.3
  • 37
    • 0030814859 scopus 로고    scopus 로고
    • Ontogeny of gonadotrophin and inhibin secretion in normal girls through puberty based on overnight serial sampling and a comparison with normal boys
    • Manasco PK, Umbach DM, Muly SM, et al. Ontogeny of gonadotrophin and inhibin secretion in normal girls through puberty based on overnight serial sampling and a comparison with normal boys. Hum Reprod. 1997;12:2108-2114.
    • (1997) Hum Reprod , vol.12 , pp. 2108-2114
    • Manasco, P.K.1    Umbach, D.M.2    Muly, S.M.3
  • 38
    • 77953914954 scopus 로고    scopus 로고
    • Neurobiological mechanisms underlying kisspeptin activation of gonadotropin-releasing hormone (GnRH) neurons at puberty
    • Clarkson J, Han SK, Liu X, Lee K, Herbison AE. Neurobiological mechanisms underlying kisspeptin activation of gonadotropin-releasing hormone (GnRH) neurons at puberty. Mol Cell Endocrinol. 2010;324:45-50.
    • (2010) Mol Cell Endocrinol , vol.324 , pp. 45-50
    • Clarkson, J.1    Han, S.K.2    Liu, X.3    Lee, K.4    Herbison, A.E.5
  • 39
    • 30944461855 scopus 로고    scopus 로고
    • Hide and run. Argininebased endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins
    • Michelsen K, Yuan H, Schwappach B. Hide and run. Argininebased endoplasmic-reticulum-sorting motifs in the assembly of heteromultimeric membrane proteins. EMBO Rep. 2005;6:717-722.
    • (2005) EMBO Rep , vol.6 , pp. 717-722
    • Michelsen, K.1    Yuan, H.2    Schwappach, B.3
  • 40
    • 78650014998 scopus 로고    scopus 로고
    • Calcium sensing receptor mutations implicated in pancreatitis and idiopathic epilepsy syndrome disrupt an arginine-rich retention motif
    • Stepanchick A, McKenna J, McGovern O, Huang Y, Breitwieser GE. Calcium sensing receptor mutations implicated in pancreatitis and idiopathic epilepsy syndrome disrupt an arginine-rich retention motif. Cell Physiol Biochem. 2010;26:363-374.
    • (2010) Cell Physiol Biochem , vol.26 , pp. 363-374
    • Stepanchick, A.1    McKenna, J.2    McGovern, O.3    Huang, Y.4    Breitwieser, G.E.5
  • 41
    • 14644387575 scopus 로고    scopus 로고
    • Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation
    • Bulenger S, Marullo S, Bouvier M. Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation. Trends Pharmacol Sci. 2005;26:131-137.
    • (2005) Trends Pharmacol Sci , vol.26 , pp. 131-137
    • Bulenger, S.1    Marullo, S.2    Bouvier, M.3
  • 42
    • 77957281362 scopus 로고    scopus 로고
    • Escorts take the lead molecular chaperones as therapeutic targets
    • Williams D, Devi LA. Escorts take the lead molecular chaperones as therapeutic targets. Prog Mol Biol Transl Sci. 2010;91:121-149.
    • (2010) Prog Mol Biol Transl Sci , vol.91 , pp. 121-149
    • Williams, D.1    Devi, L.A.2
  • 43
    • 0033667466 scopus 로고    scopus 로고
    • A trafficking checkpoint controls GABA(B) receptor heterodimerization
    • Margeta-Mitrovic M, Jan YN, Jan LY. A trafficking checkpoint controls GABA(B) receptor heterodimerization. Neuron. 2000;27: 97-106.
    • (2000) Neuron , vol.27 , pp. 97-106
    • Margeta-Mitrovic, M.1    Jan, Y.N.2    Jan, L.Y.3
  • 44
    • 56349085553 scopus 로고    scopus 로고
    • Physical association of GPR54 C-terminal with protein phosphatase 2A
    • Evans BJ, Wang Z, Mobley L, et al. Physical association of GPR54 C-terminal with protein phosphatase 2A. Biochem Biophys Res Commun. 2008;377:1067-1071.
    • (2008) Biochem Biophys Res Commun , vol.377 , pp. 1067-1071
    • Evans, B.J.1    Wang, Z.2    Mobley, L.3


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