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Volumn 12, Issue 5, 2003, Pages 1239-1250

Active and inactive orientations of the transmembrane and cytosolic domains of the erythropoietin receptor dimer

Author keywords

[No Author keywords available]

Indexed keywords

DIMERIC IONIC CONTRAST MEDIUM; ERYTHROPOIETIN RECEPTOR; HYBRID PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; STAT PROTEIN;

EID: 0344413478     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(03)00389-7     Document Type: Article
Times cited : (177)

References (47)
  • 1
    • 0036568229 scopus 로고    scopus 로고
    • Interhelical hydrogen bonds and spatial motifs in membrane proteins: Polar clamps and serine zippers
    • Adamian L., Liang J. Interhelical hydrogen bonds and spatial motifs in membrane proteins. polar clamps and serine zippers Proteins. 47:2002;209-218.
    • (2002) Proteins , vol.47 , pp. 209-218
    • Adamian, L.1    Liang, J.2
  • 2
    • 0029847652 scopus 로고    scopus 로고
    • Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching
    • Adams P.D., Engelman D.M., Brunger A.T. Improved prediction for the structure of the dimeric transmembrane domain of glycophorin A obtained through global searching. Proteins. 26:1996;257-261.
    • (1996) Proteins , vol.26 , pp. 257-261
    • Adams, P.D.1    Engelman, D.M.2    Brunger, A.T.3
  • 3
    • 0028884033 scopus 로고
    • PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo
    • Alessi D.R., Cuenda A., Cohen P., Dudley D.T., Saltiel A.R. PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J. Biol. Chem. 270:1995;27489-27494.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27489-27494
    • Alessi, D.R.1    Cuenda, A.2    Cohen, P.3    Dudley, D.T.4    Saltiel, A.R.5
  • 4
    • 2642649497 scopus 로고    scopus 로고
    • Tyrosine residues within the intracellular domain of the erythropoietin receptor mediate activation of AP-1 transcription factors
    • Bergelson S., Klingmuller U., Socolovsky M., Hsiao J.G., Lodish H.F. Tyrosine residues within the intracellular domain of the erythropoietin receptor mediate activation of AP-1 transcription factors. J. Biol. Chem. 273:1998;2396-2401.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2396-2401
    • Bergelson, S.1    Klingmuller, U.2    Socolovsky, M.3    Hsiao, J.G.4    Lodish, H.F.5
  • 5
    • 0025874677 scopus 로고
    • Erythropoietin induces Raf-1 activation and Raf-1 is required for erythropoietin-mediated proliferation
    • Carroll M.P., Spivak J.L., McMahon M., Weich N., Rapp U.R., May W.S. Erythropoietin induces Raf-1 activation and Raf-1 is required for erythropoietin-mediated proliferation. J. Biol. Chem. 266:1991;14964-14969.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14964-14969
    • Carroll, M.P.1    Spivak, J.L.2    Mcmahon, M.3    Weich, N.4    Rapp, U.R.5    May, W.S.6
  • 6
    • 0029915153 scopus 로고    scopus 로고
    • Imitation of Escherichia coli aspartate receptor signaling in engineered dimers of the cytoplasmic domain
    • Cochran A.G., Kim P.S. Imitation of Escherichia coli aspartate receptor signaling in engineered dimers of the cytoplasmic domain. Science. 271:1996;1113-1116.
    • (1996) Science , vol.271 , pp. 1113-1116
    • Cochran, A.G.1    Kim, P.S.2
  • 7
    • 0033000191 scopus 로고    scopus 로고
    • The erythropoietin receptor: Structure, activation and intracellular signal transduction
    • a
    • Constantinescu S.N., Ghaffari S., Lodish H.F. The erythropoietin receptor. structure, activation and intracellular signal transduction Trends Endocrinol. Metab. 10:1999;18-23. a.
    • (1999) Trends Endocrinol. Metab. , vol.10 , pp. 18-23
    • Constantinescu, S.N.1    Ghaffari, S.2    Lodish, H.F.3
  • 8
    • 0033564715 scopus 로고    scopus 로고
    • Activation of the erythropoietin receptor by the gp55-P viral envelope protein is determined by a single amino acid in its transmembrane domain
    • b
    • Constantinescu S.N., Liu X., Beyer W., Fallon A., Shekar S., Henis Y.I., Smith S.O., Lodish H.F. Activation of the erythropoietin receptor by the gp55-P viral envelope protein is determined by a single amino acid in its transmembrane domain. EMBO J. 18:1999;3334-3347. b.
    • (1999) EMBO J. , vol.18 , pp. 3334-3347
    • Constantinescu, S.N.1    Liu, X.2    Beyer, W.3    Fallon, A.4    Shekar, S.5    Henis, Y.I.6    Smith, S.O.7    Lodish, H.F.8
  • 9
    • 0035102191 scopus 로고    scopus 로고
    • The erythropoietin receptor cytosolic juxtamembrane domain contains an essential, precisely oriented motif
    • a
    • Constantinescu S.N., Huang L.J., Nam H., Lodish H.F. The erythropoietin receptor cytosolic juxtamembrane domain contains an essential, precisely oriented motif. Mol. Cell. 7:2001;377-385. a.
    • (2001) Mol. Cell , vol.7 , pp. 377-385
    • Constantinescu, S.N.1    Huang, L.J.2    Nam, H.3    Lodish, H.F.4
  • 10
    • 0035836645 scopus 로고    scopus 로고
    • Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain
    • b
    • Constantinescu S.N., Keren T., Socolovsky M., Nam H., Henis Y.I., Lodish H.F. Ligand-independent oligomerization of cell-surface erythropoietin receptor is mediated by the transmembrane domain. Proc. Natl. Acad. Sci. USA. 98:2001;4379-4384. b.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4379-4384
    • Constantinescu, S.N.1    Keren, T.2    Socolovsky, M.3    Nam, H.4    Henis, Y.I.5    Lodish, H.F.6
  • 11
    • 0028785505 scopus 로고
    • Phosphorylation of tyrosine 503 in the erythropoietin receptor (EpR) is essential for binding the P85 subunit of phosphatidylinositol (PI) 3-kinase and for EpR-associated PI 3-kinase activity
    • a
    • Damen J.E., Cutler R.L., Jiao H., Yi T., Krystal G. Phosphorylation of tyrosine 503 in the erythropoietin receptor (EpR) is essential for binding the P85 subunit of phosphatidylinositol (PI) 3-kinase and for EpR-associated PI 3-kinase activity. J. Biol. Chem. 270:1995;23402-23408. a.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23402-23408
    • Damen, J.E.1    Cutler, R.L.2    Jiao, H.3    Yi, T.4    Krystal, G.5
  • 12
    • 0028785893 scopus 로고
    • Tyrosine 343 in the erythropoietin receptor positively regulates erythropoietin-induced cell proliferation and Stat5 activation
    • b
    • Damen J.E., Wakao H., Miyajima A., Krosl J., Humphries R.K., Cutler R.L., Krystal G. Tyrosine 343 in the erythropoietin receptor positively regulates erythropoietin-induced cell proliferation and Stat5 activation. EMBO J. 14:1995;5557-5568. b.
    • (1995) EMBO J. , vol.14 , pp. 5557-5568
    • Damen, J.E.1    Wakao, H.2    Miyajima, A.3    Krosl, J.4    Humphries, R.K.5    Cutler, R.L.6    Krystal, G.7
  • 13
    • 0024563574 scopus 로고
    • Expression cloning of the murine erythropoietin receptor
    • D'Andrea A.D., Lodish H.F., Wong G.G. Expression cloning of the murine erythropoietin receptor. Cell. 57:1989;277-285.
    • (1989) Cell , vol.57 , pp. 277-285
    • D'andrea, A.D.1    Lodish, H.F.2    Wong, G.G.3
  • 14
    • 0028234529 scopus 로고
    • Jak-STAT pathways and transcriptional activation in response to ifn's and other extracellular signaling proteins
    • Darnell J.E., Kerr I.M., Stark G. Jak-STAT pathways and transcriptional activation in response to ifn's and other extracellular signaling proteins. Science. 264:1994;1415-1420.
    • (1994) Science , vol.264 , pp. 1415-1420
    • Darnell, J.E.1    Kerr, I.M.2    Stark, G.3
  • 15
    • 0036301006 scopus 로고    scopus 로고
    • Motifs of serine and threonine can drive association of transmembrane helices
    • Dawson J.P., Weinger J.S., Engelman D.M. Motifs of serine and threonine can drive association of transmembrane helices. J. Mol. Biol. 316:2002;799-805.
    • (2002) J. Mol. Biol. , vol.316 , pp. 799-805
    • Dawson, J.P.1    Weinger, J.S.2    Engelman, D.M.3
  • 16
    • 0036226583 scopus 로고    scopus 로고
    • Comparison of helix interactions in membrane and soluble alpha-bundle proteins
    • Eilers M., Patel A.B., Liu W., Smith S.O. Comparison of helix interactions in membrane and soluble alpha-bundle proteins. Biophys. J. 82:2002;2720-2736.
    • (2002) Biophys. J. , vol.82 , pp. 2720-2736
    • Eilers, M.1    Patel, A.B.2    Liu, W.3    Smith, S.O.4
  • 17
    • 0029742943 scopus 로고    scopus 로고
    • Activation of the erythropoietin (EPO) receptor by bivalent anti-EPO receptor antibodies
    • Elliott S., Lorenzini T., Yanagihara D., Chang D., Elliott G. Activation of the erythropoietin (EPO) receptor by bivalent anti-EPO receptor antibodies. J. Biol. Chem. 271:1996;24691-24697.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24691-24697
    • Elliott, S.1    Lorenzini, T.2    Yanagihara, D.3    Chang, D.4    Elliott, G.5
  • 19
    • 0028876304 scopus 로고
    • The signal transduction pathway of erythropoietin involves three forms of mitogen-activated protein (MAP) kinase in UT7 erythroleukemia cells
    • Gobert S., Duprez V., Lacombe C., Gisselbrecht S., Mayeux P. The signal transduction pathway of erythropoietin involves three forms of mitogen-activated protein (MAP) kinase in UT7 erythroleukemia cells. Eur. J. Biochem. 234:1995;75-83.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 75-83
    • Gobert, S.1    Duprez, V.2    Lacombe, C.3    Gisselbrecht, S.4    Mayeux, P.5
  • 21
    • 0033515557 scopus 로고    scopus 로고
    • A heptad motif of leucine residues found in membrane proteins can drive self-assembly of artificial transmembrane segments
    • Gurezka R., Laage R., Brosig B., Langosch D. A heptad motif of leucine residues found in membrane proteins can drive self-assembly of artificial transmembrane segments. J. Biol. Chem. 274:1999;9265-9270.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9265-9270
    • Gurezka, R.1    Laage, R.2    Brosig, B.3    Langosch, D.4
  • 22
    • 0028848847 scopus 로고
    • Deletions in one domain of the Friend virus-encoded membrane glycoprotein overcome host range restrictions for erythroleukemia
    • Hoatlin M.E., Ferro F. Jr., Geib R.W., Fox M.T., Kozak S.L., Kabat D. Deletions in one domain of the Friend virus-encoded membrane glycoprotein overcome host range restrictions for erythroleukemia. J. Virol. 69:1995;856-863.
    • (1995) J. Virol. , vol.69 , pp. 856-863
    • Hoatlin, M.E.1    Ferro Jr., F.2    Geib, R.W.3    Fox, M.T.4    Kozak, S.L.5    Kabat, D.6
  • 23
    • 0035694582 scopus 로고    scopus 로고
    • The N-terminal domain of Janus kinase 2 is required for Golgi processing and cell surface expression of erythropoietin receptor
    • Huang L.J., Constantinescu S.N., Lodish H.F. The N-terminal domain of Janus kinase 2 is required for Golgi processing and cell surface expression of erythropoietin receptor. Mol. Cell. 8:2001;1327-1338.
    • (2001) Mol. Cell , vol.8 , pp. 1327-1338
    • Huang, L.J.1    Constantinescu, S.N.2    Lodish, H.F.3
  • 24
    • 0035313701 scopus 로고    scopus 로고
    • The Stat family in cytokine signaling
    • Ihle J.N. The Stat family in cytokine signaling. Curr. Opin. Cell Biol. 13:2001;211-217.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 211-217
    • Ihle, J.N.1
  • 25
    • 0036098154 scopus 로고    scopus 로고
    • Identification of the human erythropoietin receptor region required for Stat1 and Stat3 activation
    • Kirito K., Nakajima K., Watanabe T., Uchida M., Tanaka M., Ozawa K., Komatsu N. Identification of the human erythropoietin receptor region required for Stat1 and Stat3 activation. Blood. 99:2002;102-110.
    • (2002) Blood , vol.99 , pp. 102-110
    • Kirito, K.1    Nakajima, K.2    Watanabe, T.3    Uchida, M.4    Tanaka, M.5    Ozawa, K.6    Komatsu, N.7
  • 26
    • 0029738317 scopus 로고    scopus 로고
    • Multiple tyrosine residues in the cytosolic domain of the erythropoietin receptor promote activation of STAT5
    • Klingmuller U., Bergelson S., Hsiao J.G., Lodish H.F. Multiple tyrosine residues in the cytosolic domain of the erythropoietin receptor promote activation of STAT5. Proc. Natl. Acad. Sci. USA. 93:1996;8324-8328.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8324-8328
    • Klingmuller, U.1    Bergelson, S.2    Hsiao, J.G.3    Lodish, H.F.4
  • 29
    • 0025004999 scopus 로고
    • Activation of cell growth by binding of Friend spleen focus-forming virus gp55 glycoprotein to the erythropoietin receptor
    • Li J.-P., D'Andrea A.D., Lodish H.F., Baltimore D. Activation of cell growth by binding of Friend spleen focus-forming virus gp55 glycoprotein to the erythropoietin receptor. Nature. 343:1990;762-764.
    • (1990) Nature , vol.343 , pp. 762-764
    • Li, J.-P.1    D'andrea, A.D.2    Lodish, H.F.3    Baltimore, D.4
  • 33
    • 0033548259 scopus 로고    scopus 로고
    • Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
    • Livnah O., Stura E.A., Middleton S.A., Johnson D.L., Jolliffe L.K., Wilson I.A. Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science. 283:1999;987-990.
    • (1999) Science , vol.283 , pp. 987-990
    • Livnah, O.1    Stura, E.A.2    Middleton, S.A.3    Johnson, D.L.4    Jolliffe, L.K.5    Wilson, I.A.6
  • 34
    • 0035963317 scopus 로고    scopus 로고
    • Identification of the transmembrane dimer interface of the bovine papillomavirus E5 protein
    • Mattoon D., Gupta K., Doyon J., Loll P.J., DiMaio D. Identification of the transmembrane dimer interface of the bovine papillomavirus E5 protein. Oncogene. 20:2001;3824-3834.
    • (2001) Oncogene , vol.20 , pp. 3824-3834
    • Mattoon, D.1    Gupta, K.2    Doyon, J.3    Loll, P.J.4    Dimaio, D.5
  • 35
    • 0028073675 scopus 로고
    • Activation of the mitogen-activated protein kinase pathway by the erythropoietin receptor
    • Miura Y., Miura O., Ihle J.N., Aoki N. Activation of the mitogen-activated protein kinase pathway by the erythropoietin receptor. J. Biol. Chem. 269:1994;29962-29969.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29962-29969
    • Miura, Y.1    Miura, O.2    Ihle, J.N.3    Aoki, N.4
  • 36
    • 0022274007 scopus 로고
    • Il-3-dependent mouse clones that express B-220 surface antigen, contain Ig genes in germ-line configuration, and generate B lymphocytes in vivo
    • Palacios R., Steinmetz M. Il-3-dependent mouse clones that express B-220 surface antigen, contain Ig genes in germ-line configuration, and generate B lymphocytes in vivo. Cell. 41:1985;727-734.
    • (1985) Cell , vol.41 , pp. 727-734
    • Palacios, R.1    Steinmetz, M.2
  • 38
    • 0345148324 scopus 로고    scopus 로고
    • A cellular reporter assay to monitor insulin receptor kinase activity based on STAT 5-dependent luciferase gene expression
    • Storz P., Doppler H., Horn-Muller J., Groner B., Pfizenmaier K., Muller G. A cellular reporter assay to monitor insulin receptor kinase activity based on STAT 5-dependent luciferase gene expression. Anal. Biochem. 276:1999;97-104.
    • (1999) Anal. Biochem. , vol.276 , pp. 97-104
    • Storz, P.1    Doppler, H.2    Horn-Muller, J.3    Groner, B.4    Pfizenmaier, K.5    Muller, G.6
  • 39
    • 0030831985 scopus 로고    scopus 로고
    • Crystal structure of a PUT3-DNA complex reveals a novel mechanism for DNA recognition by a protein containing a Zn2Cys6 binuclear cluster
    • Swaminathan K., Flynn P., Reece R.J., Marmorstein R. Crystal structure of a PUT3-DNA complex reveals a novel mechanism for DNA recognition by a protein containing a Zn2Cys6 binuclear cluster. Nat. Struct. Biol. 4:1997;751-759.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 751-759
    • Swaminathan, K.1    Flynn, P.2    Reece, R.J.3    Marmorstein, R.4
  • 41
    • 0028803402 scopus 로고
    • Journey to the surface of the cell: Fos regulation and the SRE
    • Treisman R. Journey to the surface of the cell. Fos regulation and the SRE EMBO J. 14:1995;4905-4913.
    • (1995) EMBO J. , vol.14 , pp. 4905-4913
    • Treisman, R.1
  • 42
    • 0029060110 scopus 로고
    • Interleukin 2 and erythropoietin activate STAT5/MGF via distinct pathways
    • Wakao H., Harada N., Kitamura T., Mui A., Miyajima A. Interleukin 2 and erythropoietin activate STAT5/MGF via distinct pathways. EMBO J. 14:1995;2527-2535.
    • (1995) EMBO J. , vol.14 , pp. 2527-2535
    • Wakao, H.1    Harada, N.2    Kitamura, T.3    Mui, A.4    Miyajima, A.5
  • 44
    • 0027327484 scopus 로고
    • JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin
    • Witthuhn B.A., Quelle F.W., Silvennoinen O., Yi T., Tang B., Miura O., Ihle J.N. JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin. Cell. 74:1993;227-236.
    • (1993) Cell , vol.74 , pp. 227-236
    • Witthuhn, B.A.1    Quelle, F.W.2    Silvennoinen, O.3    Yi, T.4    Tang, B.5    Miura, O.6    Ihle, J.N.7
  • 46
    • 0028880455 scopus 로고
    • Generation of committed erythroid BFU-E and CFU-E progenitors does not require erythropoietin or the erythropoietin receptor
    • Wu H., Liu X., Jaenisch R., Lodish H.F. Generation of committed erythroid BFU-E and CFU-E progenitors does not require erythropoietin or the erythropoietin receptor. Cell. 83:1995;59-67.
    • (1995) Cell , vol.83 , pp. 59-67
    • Wu, H.1    Liu, X.2    Jaenisch, R.3    Lodish, H.F.4
  • 47
    • 0025633003 scopus 로고
    • Point mutation in the exoplasmic domain of the erythropoietin receptor resulting in hormone-independent activation and tumorigenicity
    • Yoshimura A., Longmore G., Lodish H.F. Point mutation in the exoplasmic domain of the erythropoietin receptor resulting in hormone-independent activation and tumorigenicity. Nature. 348:1990;647-649.
    • (1990) Nature , vol.348 , pp. 647-649
    • Yoshimura, A.1    Longmore, G.2    Lodish, H.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.