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Volumn 188, Issue 2, 2006, Pages 251-261

A 36 residues insertion in the dimerization domain of the growth hormone receptor results in defective trafficking rather than impaired signaling

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH HORMONE RECEPTOR; JANUS KINASE 2; STAT5 PROTEIN;

EID: 33244482820     PISSN: 00220795     EISSN: None     Source Type: Journal    
DOI: 10.1677/joe.1.06252     Document Type: Article
Times cited : (29)

References (36)
  • 1
    • 0035980108 scopus 로고    scopus 로고
    • Growth hormone receptor ubiquitination, endocytosis, and degradation are independent of signal transduction via Janus kinase 2
    • Alves dos Santos CM, ten Broeke T & Strous GJ 2001 Growth hormone receptor ubiquitination, endocytosis, and degradation are independent of signal transduction via Janus kinase 2. Journal of Biological Chemistry 276 32635-32641.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 32635-32641
    • Alves dos Santos, C.M.1    ten Broeke, T.2    Strous, G.J.3
  • 5
    • 0033226506 scopus 로고    scopus 로고
    • Molecular recognition events involved in the activation of the growth hormone receptor by growth hormone
    • 1999 SN & Waters MJ
    • Behncken & Waters 1999 SN & Waters MJ 1999 Molecular recognition events involved in the activation of the growth hormone receptor by growth hormone. Journal of Molecular Recognition 12 355-362.
    • (1999) Journal of Molecular Recognition , vol.12 , pp. 355-362
    • Behncken1    Waters2
  • 7
    • 0027311301 scopus 로고
    • Mutational analysis of the intracellular domain of the human growth hormone receptor
    • Colosi P, Wong K, Leong SR & Wood WI 1993 Mutational analysis of the intracellular domain of the human growth hormone receptor. Journal of Biological Chemistry 268 12617-12623.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 12617-12623
    • Colosi, P.1    Wong, K.2    Leong, S.R.3    Wood, W.I.4
  • 8
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • Cunningham BC, Ultsch M, de Vos AM, Mulkerrin MG, Clauser KR & Wells JA 1991 Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science 254 821-825.
    • (1991) Science , vol.254 , pp. 821-825
    • Cunningham, B.C.1    Ultsch, M.2    de Vos, A.M.3    Mulkerrin, M.G.4    Clauser, K.R.5    Wells, J.A.6
  • 9
    • 0031877283 scopus 로고    scopus 로고
    • The D152H mutation found in growth hormone insensitivity syndrome impairs expression and function of human growth hormone receptor but is silent in rat receptor
    • Esposito N, Wojcik J, Chomilier J, Martini JF, Kelly PA, Finidori J & Postel-Vinay MC 1998 The D152H mutation found in growth hormone insensitivity syndrome impairs expression and function of human growth hormone receptor but is silent in rat receptor. Journal of Molecular Endocrinology 21 61-72.
    • (1998) Journal of Molecular Endocrinology , vol.21 , pp. 61-72
    • Esposito, N.1    Wojcik, J.2    Chomilier, J.3    Martini, J.F.4    Kelly, P.A.5    Finidori, J.6    Postel-Vinay, M.C.7
  • 10
    • 0033805194 scopus 로고    scopus 로고
    • Diverse deletions in the growth hormone receptor gene cause growth hormone insensitivity syndrome
    • Gastier JM, Berg MA, Vesterhus P, Reiter EO & Francke U 2000 Diverse deletions in the growth hormone receptor gene cause growth hormone insensitivity syndrome. Human Mutations 16 323-333.
    • (2000) Human Mutations , vol.16 , pp. 323-333
    • Gastier, J.M.1    Berg, M.A.2    Vesterhus, P.3    Reiter, E.O.4    Francke, U.5
  • 11
    • 0037162458 scopus 로고    scopus 로고
    • Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis
    • Gent J, van Kerkhof P, Roza M, Bu G & Strous GJ 2002 Ligand-independent growth hormone receptor dimerization occurs in the endoplasmic reticulum and is required for ubiquitin system-dependent endocytosis. PNAS 99 9858-9863.
    • (2002) PNAS , vol.99 , pp. 9858-9863
    • Gent, J.1    van Kerkhof, P.2    Roza, M.3    Bu, G.4    Strous, G.J.5
  • 13
    • 0031732473 scopus 로고    scopus 로고
    • Growth hormone (GH) insensitivity syndrome with high serum GH-binding protein levels caused by a heterozygous splice site mutation of the GH receptor gene producing a lack of intracellular domain
    • Iida K, Takahashi Y, Kaji H, Nose O, Okimura Y, Abe H & Chihara K 1998 Growth hormone (GH) insensitivity syndrome with high serum GH-binding protein levels caused by a heterozygous splice site mutation of the GH receptor gene producing a lack of intracellular domain. Journal of Clinical Endocrinology and Metabolism 83 531-537.
    • (1998) Journal of Clinical Endocrinology and Metabolism , vol.83 , pp. 531-537
    • Iida, K.1    Takahashi, Y.2    Kaji, H.3    Nose, O.4    Okimura, Y.5    Abe, H.6    Chihara, K.7
  • 17
    • 0033591392 scopus 로고    scopus 로고
    • Studies with a growth hormone antagonist and dual-fluorescent confocal microscopy demonstrate that the full-length human growth hormone receptor, but not the truncated isoform, is very rapidly internalized independent of Jak2-Stat5 signaling
    • Maamra M, Finidori J, Von Lane S, Simon S, Justice S, Webster J, Dower & Ross R 1999 Studies with a growth hormone antagonist and dual-fluorescent confocal microscopy demonstrate that the full-length human growth hormone receptor, but not the truncated isoform, is very rapidly internalized independent of Jak2-Stat5 signaling. Journal of Biological Chemistry 274 14791-14798.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 14791-14798
    • Maamra, M.1    Finidori, J.2    Von Lane, S.3    Simon, S.4    Justice, S.5    Webster, J.6    Dower7    Ross, R.8
  • 20
  • 22
    • 0031044017 scopus 로고    scopus 로고
    • A short isoform of the human growth hormone receptor functions as a dominant negative inhibitor of the full-length receptor and generates large amounts of binding protein
    • Ross RJ, Esposito N, Shen XY, Von Laue S, Chew SL, Dobson PR, Postel-Vinay MC & Finidori J 1997 A short isoform of the human growth hormone receptor functions as a dominant negative inhibitor of the full-length receptor and generates large amounts of binding protein. Molecular Endocrinology 11 265-273.
    • (1997) Molecular Endocrinology , vol.11 , pp. 265-273
    • Ross, R.J.1    Esposito, N.2    Shen, X.Y.3    Von Laue, S.4    Chew, S.L.5    Dobson, P.R.6    Postel-Vinay, M.C.7    Finidori, J.8
  • 23
    • 0035040522 scopus 로고    scopus 로고
    • Binding and functional studies with the growth hormone receptor antagonist, B2036-PEG (Pegvisomant), reveal effects of pegylation and evidence that it binds to a receptor dimer
    • Ross RJ, Leung KC, Maamra M, Bennett W, Doyle N, Waters MJ & Ho KK 2001 Binding and functional studies with the growth hormone receptor antagonist, B2036-PEG (Pegvisomant), reveal effects of pegylation and evidence that it binds to a receptor dimer. Journal of Clinical Endocrinology and Metabolism 86 1716-1723.
    • (2001) Journal of Clinical Endocrinology and Metabolism , vol.86 , pp. 1716-1723
    • Ross, R.J.1    Leung, K.C.2    Maamra, M.3    Bennett, W.4    Doyle, N.5    Waters, M.J.6    Ho, K.K.7
  • 24
    • 0032570710 scopus 로고    scopus 로고
    • Activation of chimeric and full-length growth hormone receptors by growth hormone receptor monoclonal antibodies. A specific conformational change may be required for full-length receptor signaling
    • Rowlinson SW, Behncken SN, Rowland JE, Clarkson RW, Strasburger CJ, Wu Z, Baumbach W & Waters MJ 1998 Activation of chimeric and full-length growth hormone receptors by growth hormone receptor monoclonal antibodies. A specific conformational change may be required for full-length receptor signaling. Journal of Biological Chemistry 273 5307-5314.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 5307-5314
    • Rowlinson, S.W.1    Behncken, S.N.2    Rowland, J.E.3    Clarkson, R.W.4    Strasburger, C.J.5    Wu, Z.6    Baumbach, W.7    Waters, M.J.8
  • 27
    • 0028898944 scopus 로고
    • Amino acids of the human growth hormone receptor that are required for proliferation and Jak-STAT signaling
    • Wang YD & Wood WI 1995 Amino acids of the human growth hormone receptor that are required for proliferation and Jak-STAT signaling. Molecular Endocrinology 9 303-311.
    • (1995) Molecular Endocrinology , vol.9 , pp. 303-311
    • Wang, Y.D.1    Wood, W.I.2
  • 28
    • 0026767414 scopus 로고
    • Growth hormone stimulates the tyrosine phosphorylation of 42- and 45-kDa ERK-related proteins
    • Winston LA & Bertics PJ 1992 Growth hormone stimulates the tyrosine phosphorylation of 42- and 45-kDa ERK-related proteins. Journal of Biological Chemistry 267 4747-4751.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 4747-4751
    • Winston, L.A.1    Bertics, P.J.2
  • 31
    • 0029879642 scopus 로고    scopus 로고
    • A homozygous splice site mutation affecting the intracellular domain of the growth hormone (GH) receptor resulting in Laron syndrome with elevated GH-binding protein
    • Woods KA, Fraser NC, Postel-Vinay MC, Savage MO & Clark AJ 1996 A homozygous splice site mutation affecting the intracellular domain of the growth hormone (GH) receptor resulting in Laron syndrome with elevated GH-binding protein. Journal of Clinical Endocrinology and Metabolism 81 1686-1690.
    • (1996) Journal of Clinical Endocrinology and Metabolism , vol.81 , pp. 1686-1690
    • Woods, K.A.1    Fraser, N.C.2    Postel-Vinay, M.C.3    Savage, M.O.4    Clark, A.J.5
  • 33
    • 0032755252 scopus 로고    scopus 로고
    • Disulfide linkage of growth hormone (GH) receptors (GHR) reflects GH-induced GHR dimerization. Association of JAK2 with the GHR is enhanced by receptor dimerization
    • Zhang Y, Jiang J, Kopchick JJ & Frank SJ 1999 Disulfide linkage of growth hormone (GH) receptors (GHR) reflects GH-induced GHR dimerization. Association of JAK2 with the GHR is enhanced by receptor dimerization. Journal of Biological Chemistry 274 33072-33084.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 33072-33084
    • Zhang, Y.1    Jiang, J.2    Kopchick, J.J.3    Frank, S.J.4
  • 35
    • 0034695690 scopus 로고    scopus 로고
    • Janus kinase 2-dependent activation of p38 mitogen-activated protein kinase by growth hormone. Resultant transcriptional activation of ATF-2 and CHOP, cytoskeletal re-organization and mitogenesis
    • Zhu T & Lobie PE 2000 Janus kinase 2-dependent activation of p38 mitogen-activated protein kinase by growth hormone. Resultant transcriptional activation of ATF-2 and CHOP, cytoskeletal re-organization and mitogenesis. Journal of Biological Chemistry 275 2103-2114.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 2103-2114
    • Zhu, T.1    Lobie, P.E.2
  • 36
    • 0032509512 scopus 로고    scopus 로고
    • Growth hormone stimulates the formation of a multiprotein signaling complex involving p130(Cas) and CrkII. Resultant activation of c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK)
    • Zhu T, Goh EL, LeRoith D & Lobie PE 1998 Growth hormone stimulates the formation of a multiprotein signaling complex involving p130(Cas) and CrkII. Resultant activation of c-Jun N-terminal kinase/stress-activated protein kinase (JNK/SAPK). Journal of Biological Chemistry 273 33864-33875.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 33864-33875
    • Zhu, T.1    Goh, E.L.2    LeRoith, D.3    Lobie, P.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.