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Volumn 74, Issue 5, 2006, Pages 788-797

Differential impact of intracellular carboxyl terminal domains on lipid raft localization of the murine gonadotropin-releasing hormone receptor

Author keywords

Gonadotropin releasing hormone receptor; Mechanisms of hormone action; Pituitary

Indexed keywords

G PROTEIN COUPLED RECEPTOR; GONADORELIN RECEPTOR; LUTEINIZING HORMONE RECEPTOR;

EID: 33645960686     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod.105.048157     Document Type: Article
Times cited : (15)

References (59)
  • 1
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown DA, Rose JK. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992; 68:533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 2
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Icon E. Functional rafts in cell membranes. Nature 1997; 387: 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Icon, E.2
  • 3
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Tooter D. Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 2000; 1:31-39.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Tooter, D.2
  • 4
    • 0034531095 scopus 로고    scopus 로고
    • Signaling through sphingolipid microdomains of the plasma membrane: The concept of signaling platform
    • Hoessli DC, Ilangumaran S, Soltermann A, Robinson PJ, Borisch B, Nasir UD. Signaling through sphingolipid microdomains of the plasma membrane: the concept of signaling platform. Glycoconj J 2000; 17: 191-197.
    • (2000) Glycoconj J , vol.17 , pp. 191-197
    • Hoessli, D.C.1    Ilangumaran, S.2    Soltermann, A.3    Robinson, P.J.4    Borisch, B.5    Nasir, U.D.6
  • 6
    • 0036178403 scopus 로고    scopus 로고
    • Lipid rafts and little caves. Compartmentalized signaling in membrane microdomains
    • Zajchowski LD, Robbins SM. Lipid rafts and little caves. Compartmentalized signaling in membrane microdomains. Eur J Biochem 2002; 269: 737-752.
    • (2002) Eur J Biochem , vol.269 , pp. 737-752
    • Zajchowski, L.D.1    Robbins, S.M.2
  • 7
    • 0041355360 scopus 로고    scopus 로고
    • Constitutive localization of the gonadotropin-releasing hormone (GnRH) receptor to low-density membrane microdomains is necessary for GnRH signaling to ERK
    • Navratil AM, Bliss SP, Berghom KA, Haughian JM, Farmerie TA, Graham JK, Clay CM, Roberson MS. Constitutive localization of the gonadotropin-releasing hormone (GnRH) receptor to low-density membrane microdomains is necessary for GnRH signaling to ERK. J Biol Chem 2003; 278:31593-31602.
    • (2003) J Biol Chem , vol.278 , pp. 31593-31602
    • Navratil, A.M.1    Bliss, S.P.2    Berghom, K.A.3    Haughian, J.M.4    Farmerie, T.A.5    Graham, J.K.6    Clay, C.M.7    Roberson, M.S.8
  • 8
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias DA, Violin JD, Newton AC, Tsien RY. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 2002; 296:913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 9
    • 0037036135 scopus 로고    scopus 로고
    • A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains
    • Anderson RG, Jacobson K. A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains. Science 2002; 296:1821-1825.
    • (2002) Science , vol.296 , pp. 1821-1825
    • Anderson, R.G.1    Jacobson, K.2
  • 10
    • 0037067715 scopus 로고    scopus 로고
    • Second cysteine-rich region of epidermal growth factor receptor contains targeting information for caveolae/rafts
    • Yamabhai M, Anderson RG. Second cysteine-rich region of epidermal growth factor receptor contains targeting information for caveolae/rafts. J Biol Chem 2002; 277:24843-24846.
    • (2002) J Biol Chem , vol.277 , pp. 24843-24846
    • Yamabhai, M.1    Anderson, R.G.2
  • 11
    • 0035069676 scopus 로고    scopus 로고
    • The caveolin triad: Caveolae biogenesis, cholesterol trafficking, and signal transduction
    • Schlegel A, Lisanti MP. The caveolin triad: caveolae biogenesis, cholesterol trafficking, and signal transduction. Cytokine Growth Factor Rev 2001; 12:41-51.
    • (2001) Cytokine Growth Factor Rev , vol.12 , pp. 41-51
    • Schlegel, A.1    Lisanti, M.P.2
  • 12
    • 0035979221 scopus 로고    scopus 로고
    • The sorbin homology domain: A motif for the targeting of proteins to lipid rafts
    • Kimura A, Baumann CA, Chiang SH, Saltiel AR. The sorbin homology domain: a motif for the targeting of proteins to lipid rafts. Proc Natl Acad Sci U S A 2001; 98:9098-9103.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 9098-9103
    • Kimura, A.1    Baumann, C.A.2    Chiang, S.H.3    Saltiel, A.R.4
  • 13
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 1998; 14:111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 14
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether U. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr Rev 2000; 21:90-113.
    • (2000) Endocr Rev , vol.21 , pp. 90-113
    • Gether, U.1
  • 16
    • 0034825632 scopus 로고    scopus 로고
    • Palmitoylation of the luteinizing hormone/human chorionic gonadotropin receptor regulates receptor interaction with the arrestin-mediated internalization pathway
    • Munshi UM, Peegel H, Menon KM. Palmitoylation of the luteinizing hormone/human chorionic gonadotropin receptor regulates receptor interaction with the arrestin-mediated internalization pathway. Eur J Biochem 2001; 268:1631-1639.
    • (2001) Eur J Biochem , vol.268 , pp. 1631-1639
    • Munshi, U.M.1    Peegel, H.2    Menon, K.M.3
  • 17
    • 0031732763 scopus 로고    scopus 로고
    • Palmitoylation of human thyrotropin receptor: Slower intracellular trafficking of the palmitoylation-defective mutant
    • Tanaka K, Nagayama Y, Nishihara E, Namba H, Yamashita S, Niwa M. Palmitoylation of human thyrotropin receptor: slower intracellular trafficking of the palmitoylation-defective mutant. Endocrinology 1998; 139:803-806.
    • (1998) Endocrinology , vol.139 , pp. 803-806
    • Tanaka, K.1    Nagayama, Y.2    Nishihara, E.3    Namba, H.4    Yamashita, S.5    Niwa, M.6
  • 18
    • 0028092770 scopus 로고
    • Gonadotropin-releasing hormone receptors: Structure and signal transduction pathways
    • Stojilkovic SS, Reinhart J, Catt KJ. Gonadotropin-releasing hormone receptors: structure and signal transduction pathways. Endocr Rev 1994; 15:462-499.
    • (1994) Endocr Rev , vol.15 , pp. 462-499
    • Stojilkovic, S.S.1    Reinhart, J.2    Catt, K.J.3
  • 19
    • 0030937284 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand interaction with the gonadotropin- releasing hormone receptor
    • Sealfon SC, Weinstein H, Millar RP. Molecular mechanisms of ligand interaction with the gonadotropin-releasing hormone receptor. Endocr Rev 1997; 18:180-205.
    • (1997) Endocr Rev , vol.18 , pp. 180-205
    • Sealfon, S.C.1    Weinstein, H.2    Millar, R.P.3
  • 21
    • 0031393975 scopus 로고    scopus 로고
    • Molecular mechanisms of G protein-coupled receptor signaling: Role of G protein-coupled receptor kinases and arrestins in receptor desensitization and resensitization
    • Zhang J, Ferguson SS, Barak LS, Aber MJ, Giros B, Lefkowitz RJ, Caron MG. Molecular mechanisms of G protein-coupled receptor signaling: role of G protein-coupled receptor kinases and arrestins in receptor desensitization and resensitization. Receptors Channels 1997; 5:193-199.
    • (1997) Receptors Channels , vol.5 , pp. 193-199
    • Zhang, J.1    Ferguson, S.S.2    Barak, L.S.3    Aber, M.J.4    Giros, B.5    Lefkowitz, R.J.6    Caron, M.G.7
  • 22
    • 0035101820 scopus 로고    scopus 로고
    • Evolving concepts in G protein-coupled receptor endocytosis: The role in receptor desensitization and signaling
    • Ferguson SS. Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling. Pharmacol Rev 2001; 53:1-24.
    • (2001) Pharmacol Rev , vol.53 , pp. 1-24
    • Ferguson, S.S.1
  • 23
    • 0036892176 scopus 로고    scopus 로고
    • Two gonadotropin-releasing hormone receptors in the African catfish: No differences in ligand selectivity, but differences in tissue distribution
    • Bogerd J, Diepenbroek WB, Hund E, van Oosterhout F, Teves AC, Leurs R, Blomenrohr M. Two gonadotropin-releasing hormone receptors in the African catfish: no differences in ligand selectivity, but differences in tissue distribution. Endocrinology 2002; 143:4673-4682.
    • (2002) Endocrinology , vol.143 , pp. 4673-4682
    • Bogerd, J.1    Diepenbroek, W.B.2    Hund, E.3    Van Oosterhout, F.4    Teves, A.C.5    Leurs, R.6    Blomenrohr, M.7
  • 24
    • 0033515025 scopus 로고    scopus 로고
    • Two gonadotropin-releasing hormone receptor subtypes with distinct ligand selectivity and differential distribution in brain and pituitary in the goldfish (Carassius auratus)
    • Illing N, Troskie BE, Nahomiak CS, Hapgood JP, Peter RE, Millar RP. Two gonadotropin-releasing hormone receptor subtypes with distinct ligand selectivity and differential distribution in brain and pituitary in the goldfish (Carassius auratus). Proc Natl Acad Sci U S A 1999; 96:2526-2531.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 2526-2531
    • Illing, N.1    Troskie, B.E.2    Nahomiak, C.S.3    Hapgood, J.P.4    Peter, R.E.5    Millar, R.P.6
  • 25
    • 0035896512 scopus 로고    scopus 로고
    • A chicken gonadotropin-releasing hormone receptor that confers agonist activity to mammalian antagonists. Identification of D-Lys(6) in the ligand and extracellular loop two of the receptor as determinants
    • Sun YM, Flanagan CA, Illing N, Ott TR, Sellar R, Fromme BJ, Hapgood J, Sharp P, Sealfon SC, Millar RP. A chicken gonadotropin-releasing hormone receptor that confers agonist activity to mammalian antagonists. Identification of D-Lys(6) in the ligand and extracellular loop two of the receptor as determinants. J Biol Chem 2001; 276:7754-7761.
    • (2001) J Biol Chem , vol.276 , pp. 7754-7761
    • Sun, Y.M.1    Flanagan, C.A.2    Illing, N.3    Ott, T.R.4    Sellar, R.5    Fromme, B.J.6    Hapgood, J.7    Sharp, P.8    Sealfon, S.C.9    Millar, R.P.10
  • 26
    • 0034456241 scopus 로고    scopus 로고
    • Complementary deoxyribonucleic acid cloning, gene expression, and ligand selectivity of a novel gonadotropin-releasing hormone receptor expressed in the pituitary and midbrain of Xenopus laevis
    • Troskie BE, Hapgood JP, Millar RP, Illing N. Complementary deoxyribonucleic acid cloning, gene expression, and ligand selectivity of a novel gonadotropin-releasing hormone receptor expressed in the pituitary and midbrain of Xenopus laevis. Endocrinology 2000; 141:1764-1771.
    • (2000) Endocrinology , vol.141 , pp. 1764-1771
    • Troskie, B.E.1    Hapgood, J.P.2    Millar, R.P.3    Illing, N.4
  • 27
    • 0032496280 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone receptors with intracellular carboxyl-terminal tails undergo acute desensitization of total inositol phosphate production and exhibit accelerated internalization kinetics
    • Heding A, Vrecl M, Bogerd J, McGregor A, Sellar R, Taylor PL, Eidne KA. Gonadotropin-releasing hormone receptors with intracellular carboxyl-terminal tails undergo acute desensitization of total inositol phosphate production and exhibit accelerated internalization kinetics. J Biol Chem 1998; 273:11472-11477.
    • (1998) J Biol Chem , vol.273 , pp. 11472-11477
    • Heding, A.1    Vrecl, M.2    Bogerd, J.3    McGregor, A.4    Sellar, R.5    Taylor, P.L.6    Eidne, K.A.7
  • 28
    • 0345045562 scopus 로고    scopus 로고
    • Pivotal role for the cytoplasmic carboxyl-terminal tail of a nonmammalian gonadotropin-releasing hormone receptor in cell surface expression, ligand binding, and receptor phosphorylation and internalization
    • Blomenrohr M, Heding A, Sellar R, Leurs R, Bogerd J, Eidne KA, Willars GB. Pivotal role for the cytoplasmic carboxyl-terminal tail of a nonmammalian gonadotropin-releasing hormone receptor in cell surface expression, ligand binding, and receptor phosphorylation and internalization. Mol Pharmacol 1999; 56:1229-1237.
    • (1999) Mol Pharmacol , vol.56 , pp. 1229-1237
    • Blomenrohr, M.1    Heding, A.2    Sellar, R.3    Leurs, R.4    Bogerd, J.5    Eidne, K.A.6    Willars, G.B.7
  • 29
    • 0033570130 scopus 로고    scopus 로고
    • Lack of a C-terminal tail in the mammalian gonadotropin-releasing hormone receptor confers resistance to agonist-dependent phosphorylation and rapid desensitization
    • Willars GB, Heding A, Vrecl M, Sellar R, Blomenrohr M, Nahorski SR, Eidne KA. Lack of a C-terminal tail in the mammalian gonadotropin-releasing hormone receptor confers resistance to agonist-dependent phosphorylation and rapid desensitization. J Biol Chem 2000; 274: 30146-30153.
    • (2000) J Biol Chem , vol.274 , pp. 30146-30153
    • Willars, G.B.1    Heding, A.2    Vrecl, M.3    Sellar, R.4    Blomenrohr, M.5    Nahorski, S.R.6    Eidne, K.A.7
  • 30
    • 0036000180 scopus 로고    scopus 로고
    • The gonadotrophin-releasing hormone receptor: Signaling, cycling, and desensitization
    • McArdle CA, Franklin J, Green L, Hislop JN. The gonadotrophin-releasing hormone receptor: signaling, cycling, and desensitization. Arch Physiol Biochem 2002; 110:113-122.
    • (2002) Arch Physiol Biochem , vol.110 , pp. 113-122
    • McArdle, C.A.1    Franklin, J.2    Green, L.3    Hislop, J.N.4
  • 31
    • 0033628188 scopus 로고    scopus 로고
    • Internalization kinetics of the gonadotropin-releasing hormone (GnRH) receptor
    • Vrecl M, Heding A, Hanyaloglu A, Taylor PL, Eidne KA. Internalization kinetics of the gonadotropin-releasing hormone (GnRH) receptor. Pflugers Arch 2000; 439:R19-R20.
    • (2000) Pflugers Arch , vol.439
    • Vrecl, M.1    Heding, A.2    Hanyaloglu, A.3    Taylor, P.L.4    Eidne, K.A.5
  • 32
    • 0033603021 scopus 로고    scopus 로고
    • The tail of the gonadotrophin-releasing hormone receptor: Desensitization at, and distal to, G protein-coupled receptors
    • McArdle CA, Davidson JS, Willars GB. The tail of the gonadotrophin- releasing hormone receptor: desensitization at, and distal to, G protein-coupled receptors. Mol Cell Endocrinol 1999; 151:129-136.
    • (1999) Mol Cell Endocrinol , vol.151 , pp. 129-136
    • McArdle, C.A.1    Davidson, J.S.2    Willars, G.B.3
  • 33
    • 0032230140 scopus 로고    scopus 로고
    • Addition of catfish gonadotropin-releasing hormone (GnRH) receptor intracellular carboxyl-terminal tail to rat GnRH receptor alters receptor expression and regulation
    • Lin X, Janovick JA, Brothers S, Blomenrohr M, Bogerd J, Conn PM. Addition of catfish gonadotropin-releasing hormone (GnRH) receptor intracellular carboxyl-terminal tail to rat GnRH receptor alters receptor expression and regulation. Mol Endocrinol 1998; 12:161-171.
    • (1998) Mol Endocrinol , vol.12 , pp. 161-171
    • Lin, X.1    Janovick, J.A.2    Brothers, S.3    Blomenrohr, M.4    Bogerd, J.5    Conn, P.M.6
  • 34
    • 0034463035 scopus 로고    scopus 로고
    • The rat gonadotropin-releasing hormone receptor internalizes via a β-arrestin-independent, but dynamin-dependent, pathway: Addition of a carboxyl-terminal tail confers β-arrestin dependency
    • Heding A, Vrecl M, Hanyaloglu A, Sellar R, Taylor PL, Eidne KA. The rat gonadotropin-releasing hormone receptor internalizes via a β-arrestin- independent, but dynamin-dependent, pathway: addition of a carboxyl-terminal tail confers β-arrestin dependency. Endocrinology 2000; 141: 299-306.
    • (2000) Endocrinology , vol.141 , pp. 299-306
    • Heding, A.1    Vrecl, M.2    Hanyaloglu, A.3    Sellar, R.4    Taylor, P.L.5    Eidne, K.A.6
  • 35
    • 0344739567 scopus 로고    scopus 로고
    • Self-association and raft localization of functional luteinizing hormone receptors
    • Roess DA, Smith SM. Self-association and raft localization of functional luteinizing hormone receptors. Biol Reprod 2003; 69:1765-1770.
    • (2003) Biol Reprod , vol.69 , pp. 1765-1770
    • Roess, D.A.1    Smith, S.M.2
  • 36
    • 0041920691 scopus 로고    scopus 로고
    • Multiple determinants for rapid agonist-induced internalization of a nonmammalian gonadotropin-releasing hormone receptor: A putative palmitoylation site and threonine doublet within the carboxyl-terminal tail Are critical
    • Pawson AJ, Maudsley SR, Lopes J, Katz AA, Sun YM, Davidson JS, Millar RP. Multiple determinants for rapid agonist-induced internalization of a nonmammalian gonadotropin-releasing hormone receptor: a putative palmitoylation site and threonine doublet within the carboxyl-terminal tail Are critical. Endocrinology 2003; 144:3860-3871.
    • (2003) Endocrinology , vol.144 , pp. 3860-3871
    • Pawson, A.J.1    Maudsley, S.R.2    Lopes, J.3    Katz, A.A.4    Sun, Y.M.5    Davidson, J.S.6    Millar, R.P.7
  • 37
    • 4644341495 scopus 로고    scopus 로고
    • Serine residues 338 and 339 in the carboxyl-terminal tail of the type II gonadotropin-releasing hormone receptor are critical for β-arrestin- independent internalization
    • Ronacher K, Matsiliza N, Nkwanyana N, Pawson AJ, Adam T, Flanagan CA, Millar RP, Katz AA. Serine residues 338 and 339 in the carboxyl-terminal tail of the type II gonadotropin-releasing hormone receptor are critical for β-arrestin-independent internalization. Endocrinology 2004; 145:4480-4488.
    • (2004) Endocrinology , vol.145 , pp. 4480-4488
    • Ronacher, K.1    Matsiliza, N.2    Nkwanyana, N.3    Pawson, A.J.4    Adam, T.5    Flanagan, C.A.6    Millar, R.P.7    Katz, A.A.8
  • 38
    • 0037872036 scopus 로고    scopus 로고
    • Analysis of the mobility of signaling molecules in lymphocytes using fluorescence photobleaching techniques
    • Tanimura N, Nagafuku M, Liddicoat DR, Hamaoka T, Kosugi A. Analysis of the mobility of signaling molecules in lymphocytes using fluorescence photobleaching techniques. Sci STKE 2003; 2003:110.
    • (2003) Sci STKE , vol.2003 , pp. 110
    • Tanimura, N.1    Nagafuku, M.2    Liddicoat, D.R.3    Hamaoka, T.4    Kosugi, A.5
  • 39
    • 0029912981 scopus 로고    scopus 로고
    • Copurification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains
    • Song KS, Li S, Okamoto T, Quilliam LA, Sargiacomo M, Lisanti MP. Copurification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains. J Biol Chem 1996; 271:9690-9697.
    • (1996) J Biol Chem , vol.271 , pp. 9690-9697
    • Song, K.S.1    Li, S.2    Okamoto, T.3    Quilliam, L.A.4    Sargiacomo, M.5    Lisanti, M.P.6
  • 40
    • 0018743533 scopus 로고
    • GNRH interaction with anterior pituitary. I. Determination of the affinity and number of receptors for GNRH in ovine anterior pituitary
    • Wagner TO, Adams TE, Nett TM. GNRH interaction with anterior pituitary. I. Determination of the affinity and number of receptors for GNRH in ovine anterior pituitary. Biol Reprod 1979; 20:140-149.
    • (1979) Biol Reprod , vol.20 , pp. 140-149
    • Wagner, T.O.1    Adams, T.E.2    Nett, T.M.3
  • 41
    • 0026591515 scopus 로고
    • Effects of truncations of the cytoplasmic tail of the luteinizing hormone/chorionic gonadotropin receptor on receptor-mediated hormone internalization
    • Rodriguez MC, Xie Y-B, Wang H, Collison K, Segaloff DL. Effects of truncations of the cytoplasmic tail of the luteinizing hormone/chorionic gonadotropin receptor on receptor-mediated hormone internalization. Mol Endocrinol 1992; 6:327-336.
    • (1992) Mol Endocrinol , vol.6 , pp. 327-336
    • Rodriguez, M.C.1    Xie, Y.-B.2    Wang, H.3    Collison, K.4    Segaloff, D.L.5
  • 42
    • 0037370534 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase activation of activator protein-1 underlies homologous regulation of the gonadotropin-releasing hormone receptor gene in α T3-1 cells
    • Ellsworth BS, White BR, Burns AT, Cherrington BD, Otis AM, Clay CM. c-Jun N-terminal kinase activation of activator protein-1 underlies homologous regulation of the gonadotropin-releasing hormone receptor gene in α T3-1 cells. Endocrinology 2003; 144:839-849.
    • (2003) Endocrinology , vol.144 , pp. 839-849
    • Ellsworth, B.S.1    White, B.R.2    Burns, A.T.3    Cherrington, B.D.4    Otis, A.M.5    Clay, C.M.6
  • 43
    • 0036241442 scopus 로고    scopus 로고
    • Signaling, cycling, and desensitization of gonadotrophin-releasing hormone receptors
    • McArdle CA, Franklin J, Green L, Hislop JN. Signaling, cycling, and desensitization of gonadotrophin-releasing hormone receptors. J Endocrinol 2002; 173:1-11.
    • (2002) J Endocrinol , vol.173 , pp. 1-11
    • McArdle, C.A.1    Franklin, J.2    Green, L.3    Hislop, J.N.4
  • 44
    • 0035116362 scopus 로고    scopus 로고
    • Internalization rates of murine and ovine gonadotropin-releasing hormone receptors
    • Hashizume T, Yang WH, Clay CM, Nett TM. Internalization rates of murine and ovine gonadotropin-releasing hormone receptors. Biol Reprod 2001; 64:898-903.
    • (2001) Biol Reprod , vol.64 , pp. 898-903
    • Hashizume, T.1    Yang, W.H.2    Clay, C.M.3    Nett, T.M.4
  • 46
    • 0032961873 scopus 로고    scopus 로고
    • Characterization of an intrinsically fluorescent gonadotropin-releasing hormone receptor and effects of ligand binding on receptor lateral diffusion
    • Nelson S, Horvat RD, Malvey J, Roess DA, Barisas BG, Clay CM. Characterization of an intrinsically fluorescent gonadotropin-releasing hormone receptor and effects of ligand binding on receptor lateral diffusion. Endocrinology 1999; 140:950-957.
    • (1999) Endocrinology , vol.140 , pp. 950-957
    • Nelson, S.1    Horvat, R.D.2    Malvey, J.3    Roess, D.A.4    Barisas, B.G.5    Clay, C.M.6
  • 47
    • 0842313243 scopus 로고    scopus 로고
    • Evolved regulation of gonadotropin-releasing hormone receptor cell surface expression
    • Janovick JA, Ulloa-Aguirre A, Conn PM. Evolved regulation of gonadotropin-releasing hormone receptor cell surface expression. Endocrine 2003; 22:317-327.
    • (2003) Endocrine , vol.22 , pp. 317-327
    • Janovick, J.A.1    Ulloa-Aguirre, A.2    Conn, P.M.3
  • 48
    • 0028872763 scopus 로고
    • The lutropin/choriogonadotropin receptor is palmitoylated at intracellular cysteine residues
    • Zhu H, Wang H, Ascoli M. The lutropin/choriogonadotropin receptor is palmitoylated at intracellular cysteine residues. Mol Endocrinol 1995; 9: 141-150.
    • (1995) Mol Endocrinol , vol.9 , pp. 141-150
    • Zhu, H.1    Wang, H.2    Ascoli, M.3
  • 49
    • 0032541044 scopus 로고    scopus 로고
    • Mutation of individual serine residues in the C-terminal tail of the lutropin/choriogonadotropin receptor reveal distinct structural requirements for agonist-induced uncoupling and agonist-induced internalization
    • Lazari MF, Bertrand JE, Nakamura K, Liu X, Krupnick JG, Benovic JL, Ascoli M. Mutation of individual serine residues in the C-terminal tail of the lutropin/choriogonadotropin receptor reveal distinct structural requirements for agonist-induced uncoupling and agonist-induced internalization. J Biol Chem 1998; 273:18316-18324.
    • (1998) J Biol Chem , vol.273 , pp. 18316-18324
    • Lazari, M.F.1    Bertrand, J.E.2    Nakamura, K.3    Liu, X.4    Krupnick, J.G.5    Benovic, J.L.6    Ascoli, M.7
  • 50
    • 0035947557 scopus 로고    scopus 로고
    • Casein kinase II sites in the intracellular C-terminal domain of the thyrotropin-releasing hormone receptor and chimeric gonadotropin-releasing hormone receptors contribute to β-arrestin-dependent internalization
    • Hanyaloglu AC, Vrecl M, Kroeger KM, Miles LE, Qian H, Thomas WG, Eidne KA. Casein kinase II sites in the intracellular C-terminal domain of the thyrotropin-releasing hormone receptor and chimeric gonadotropin-releasing hormone receptors contribute to β-arrestin-dependent internalization. J Biol Chem 2001; 276:18066-18074.
    • (2001) J Biol Chem , vol.276 , pp. 18066-18074
    • Hanyaloglu, A.C.1    Vrecl, M.2    Kroeger, K.M.3    Miles, L.E.4    Qian, H.5    Thomas, W.G.6    Eidne, K.A.7
  • 51
    • 0242721361 scopus 로고    scopus 로고
    • Multifaceted roles of β-arrestins in the regulation of seven-membrane-spanning receptor trafficking and signaling
    • Shenoy SK, Lefkowitz RJ. Multifaceted roles of β-arrestins in the regulation of seven-membrane-spanning receptor trafficking and signaling. Biochem J 2003; 375:503-515.
    • (2003) Biochem J , vol.375 , pp. 503-515
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 52
    • 0344393408 scopus 로고    scopus 로고
    • Regulation of MAP kinase signaling modules by scaffold proteins in mammals
    • Morrison DK, Davis RJ. Regulation of MAP kinase signaling modules by scaffold proteins in mammals. Annu Rev Cell Dev Biol 2003; 19:91-118.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 91-118
    • Morrison, D.K.1    Davis, R.J.2
  • 53
    • 0345564815 scopus 로고    scopus 로고
    • Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin
    • Kwik J, Boyle S, Fooksman D, Margolis L, Sheetz MP, Edidin M. Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate- dependent organization of cell actin. Proc Natl Acad Sci U S A 2003; 100:13964-13969.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 13964-13969
    • Kwik, J.1    Boyle, S.2    Fooksman, D.3    Margolis, L.4    Sheetz, M.P.5    Edidin, M.6
  • 54
    • 0035054915 scopus 로고    scopus 로고
    • Luteinizing hormone receptors are self-associated in slowly diffusing complexes during receptor desensitization
    • Horvat RD, Barisas BG, Roess DA. Luteinizing hormone receptors are self-associated in slowly diffusing complexes during receptor desensitization. Mol Endocrinol 2001; 15:534-542.
    • (2001) Mol Endocrinol , vol.15 , pp. 534-542
    • Horvat, R.D.1    Barisas, B.G.2    Roess, D.A.3
  • 55
    • 20744433934 scopus 로고    scopus 로고
    • Ligand-induced partitioning of human CXCR1 chemokine receptors with lipid raft microenvironments facilitates G protein-dependent signaling
    • Jiao X, Zhang N, Xu X, Oppenheim JJ, Jin T. Ligand-induced partitioning of human CXCR1 chemokine receptors with lipid raft microenvironments facilitates G protein-dependent signaling. Mol Cell Biol 2005; 25:5752-5762.
    • (2005) Mol Cell Biol , vol.25 , pp. 5752-5762
    • Jiao, X.1    Zhang, N.2    Xu, X.3    Oppenheim, J.J.4    Jin, T.5
  • 57
    • 0036841874 scopus 로고    scopus 로고
    • Triton promotes domain formation in lipid raft mixtures
    • Heerklotz H. Triton promotes domain formation in lipid raft mixtures. Biophys J 2002; 83:2693-2701.
    • (2002) Biophys J , vol.83 , pp. 2693-2701
    • Heerklotz, H.1
  • 58
    • 15544387138 scopus 로고    scopus 로고
    • Consequences of lipid raft association on G protein-coupled receptor function
    • Becher A, McIlhinney RA. Consequences of lipid raft association on G protein-coupled receptor function. Biochem Soc Symp 2005; 151-164.
    • (2005) Biochem Soc Symp , pp. 151-164
    • Becher, A.1    McIlhinney, R.A.2
  • 59
    • 24344468190 scopus 로고    scopus 로고
    • Gonadotropin-releasing hormone induction of extracellular-signal regulated kinase is blocked by inhibition of calmodulin
    • 2005
    • Roberson MS, Bliss SP, Xie J, Navratil AM, Farmerie TA, Wolfe MW, Clay CM. 2005. Gonadotropin-releasing hormone induction of extracellular-signal regulated kinase is blocked by inhibition of calmodulin. Mol Endocrinol 2005; 19:2412-2423.
    • (2005) Mol Endocrinol , vol.19 , pp. 2412-2423
    • Roberson, M.S.1    Bliss, S.P.2    Xie, J.3    Navratil, A.M.4    Farmerie, T.A.5    Wolfe, M.W.6    Clay, C.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.