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Volumn 109, Issue 7, 2012, Pages 2503-2508

Structural reorganization of the interleukin-7 signaling complex

Author keywords

Biophysics; Cancer mutations; Homodimerization; X ray crystallography

Indexed keywords

HOMODIMER; INTERLEUKIN 7 RECEPTOR ALPHA; TERNARY COMPLEX FACTOR;

EID: 84857131673     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1116582109     Document Type: Article
Times cited : (53)

References (40)
  • 1
    • 33846632842 scopus 로고    scopus 로고
    • Interleukin-7 receptor expression: Intelligent design
    • DOI 10.1038/nri2023, PII NRI2023
    • Mazzucchelli R, Durum SK (2007) Interleukin-7 receptor expression: Intelligent design. Nat Rev Immunol 7(2):144-154. (Pubitemid 46178275)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.2 , pp. 144-154
    • Mazzucchelli, R.1    Durum, S.K.2
  • 2
    • 0037119351 scopus 로고    scopus 로고
    • Cytokine and cytokine receptor pleiotropy and redundancy
    • DOI 10.1074/jbc.R200003200
    • Ozaki K, Leonard WJ (2002) Cytokine and cytokine receptor pleiotropy and redundancy. J Biol Chem 277:29355-29358. (Pubitemid 41079217)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.33 , pp. 29355-29358
    • Ozaki, K.1    Leonard, W.J.2
  • 3
    • 9644295710 scopus 로고    scopus 로고
    • c-dependent cytokines interleukins 2, 4, 7, 9, 15, and 21, and their signaling pathways
    • DOI 10.1111/j.0105-2896.2004.00203.x
    • Kovanen PE, Leonard WJ (2004) Cytokines and immunodeficiency diseases: Critical roles of the γ(c)-dependent cytokines interleukins 2, 4, 7, 9, 15, and 21, and their signaling pathways. Immunol Rev 202(1):67-83. (Pubitemid 39576905)
    • (2004) Immunological Reviews , vol.202 , pp. 67-83
    • Kovanen, P.E.1    Leonard, W.J.2
  • 7
    • 0035469821 scopus 로고    scopus 로고
    • Interleukin-7 promotes survival and cell cycle progression of T-cell acute lymphoblastic leukemia cells by downregulating the cyclin-dependent kinase inhibitor p27(kip1)
    • Barata JT, Cardoso AA, Nadler LM, Boussiotis VA (2001) Interleukin-7 promotes survival and cell cycle progression of T-cell acute lymphoblastic leukemia cells by downregulating the cyclin-dependent kinase inhibitor p27(kip1). Blood 98:1524-1531.
    • (2001) Blood , vol.98 , pp. 1524-1531
    • Barata, J.T.1    Cardoso, A.A.2    Nadler, L.M.3    Boussiotis, V.A.4
  • 8
    • 80053385665 scopus 로고    scopus 로고
    • Oncogenic IL7R gain-of-function mutations in childhood T-cell acute lymphoblastic leukemia
    • Zenatti PP, et al. (2011) Oncogenic IL7R gain-of-function mutations in childhood T-cell acute lymphoblastic leukemia. Nat Genet 43:932-939.
    • (2011) Nat Genet , vol.43 , pp. 932-939
    • Zenatti, P.P.1
  • 9
    • 67649876115 scopus 로고    scopus 로고
    • New insights into the regulation of T cells by γ(c) family cytokines
    • Rochman Y, Spolski R, Leonard WJ (2009) New insights into the regulation of T cells by γ(c) family cytokines. Nat Rev Immunol 9:480-490.
    • (2009) Nat Rev Immunol , vol.9 , pp. 480-490
    • Rochman, Y.1    Spolski, R.2    Leonard, W.J.3
  • 10
    • 0025350049 scopus 로고
    • Cloning of the human and murine interleukin-7 receptors: Demonstration of a soluble form and homology to a new receptor superfamily
    • Goodwin RG, et al. (1990) Cloning of the human and murine interleukin-7 receptors: Demonstration of a soluble form and homology to a new receptor superfamily. Cell 60:941-951.
    • (1990) Cell , vol.60 , pp. 941-951
    • Goodwin, R.G.1
  • 11
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • Wells JA (1996) Binding in the growth hormone receptor complex. Proc Natl Acad Sci USA 93(1):1-6.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.1 , pp. 1-6
    • Wells, J.A.1
  • 12
    • 67649158212 scopus 로고    scopus 로고
    • Identification and biochemical characterization of human plasma soluble IL-7R: Lower concentrations in HIV-1-infected patients
    • Rose T, Lambotte O, Pallier C, Delfraissy JF, Colle JH (2009) Identification and biochemical characterization of human plasma soluble IL-7R: Lower concentrations in HIV-1-infected patients. J Immunol 182:7389-7397.
    • (2009) J Immunol , vol.182 , pp. 7389-7397
    • Rose, T.1    Lambotte, O.2    Pallier, C.3    Delfraissy, J.F.4    Colle, J.H.5
  • 13
    • 77952033674 scopus 로고    scopus 로고
    • Interleukin-7 compartmentalizes its receptor signaling complex to initiate CD4 T lymphocyte response
    • Rose T, et al. (2010) Interleukin-7 compartmentalizes its receptor signaling complex to initiate CD4 T lymphocyte response. J Biol Chem 285:14898-14908.
    • (2010) J Biol Chem , vol.285 , pp. 14898-14908
    • Rose, T.1
  • 14
    • 77958498185 scopus 로고    scopus 로고
    • IL-2 induces conformational changes in its preassembled receptor core, which then migrates in lipid raft and binds to the cytoskeleton meshwork
    • Pillet AH, et al. (2010) IL-2 induces conformational changes in its preassembled receptor core, which then migrates in lipid raft and binds to the cytoskeleton meshwork. J Mol Biol 403:671-692.
    • (2010) J Mol Biol , vol.403 , pp. 671-692
    • Pillet, A.H.1
  • 15
    • 0029796365 scopus 로고    scopus 로고
    • Homodimerization of interleukin-4 receptor α chain can induce intracellular signaling
    • Kammer W, et al. (1996) Homodimerization of interleukin-4 receptor α chain can induce intracellular signaling. J Biol Chem 271:23634-23637.
    • (1996) J Biol Chem , vol.271 , pp. 23634-23637
    • Kammer, W.1
  • 16
    • 57749119532 scopus 로고    scopus 로고
    • Ligand-independent homomeric and heteromeric complexes between interleukin-2 or -9 receptor subunits and the γ chain
    • Malka Y, et al. (2008) Ligand-independent homomeric and heteromeric complexes between interleukin-2 or -9 receptor subunits and the γ chain. J Biol Chem 283: 33569-33577.
    • (2008) J Biol Chem , vol.283 , pp. 33569-33577
    • Malka, Y.1
  • 17
    • 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 HF (1990) Point mutation in the exoplasmic domain of the erythropoietin receptor resulting in hormone-independent activation and tumorigenicity. Nature 348:647-649. (Pubitemid 120015129)
    • (1990) Nature , vol.348 , Issue.6302 , pp. 647-649
    • Yoshimura, A.1    Longmore, G.2    Lodish, H.F.3
  • 18
    • 77955334994 scopus 로고    scopus 로고
    • Cytokine-receptor interactions as drug targets
    • Schreiber G, Walter MR (2010) Cytokine-receptor interactions as drug targets. Curr Opin Chem Biol 14:511-519.
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 511-519
    • Schreiber, G.1    Walter, M.R.2
  • 19
    • 58149193349 scopus 로고    scopus 로고
    • Structural and biophysical studies of the human IL-7/IL-7Rα complex
    • McElroy CA, Dohm JA, Walsh ST (2009) Structural and biophysical studies of the human IL-7/IL-7Rα complex. Structure 17:54-65.
    • (2009) Structure , vol.17 , pp. 54-65
    • McElroy, C.A.1    Dohm, J.A.2    Walsh, S.T.3
  • 20
    • 27944505913 scopus 로고    scopus 로고
    • c receptors
    • DOI 10.1126/science.1117893
    • Wang X, Rickert M, Garcia KC (2005) Structure of the quaternary complex of interleukin-2 with its α, β, and γc receptors. Science 310:1159-1163. (Pubitemid 41681737)
    • (2005) Science , vol.310 , Issue.5751 , pp. 1159-1163
    • Wang, X.1    Rickert, M.2    Garcia, K.C.3
  • 21
    • 0033548259 scopus 로고    scopus 로고
    • Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation
    • Livnah O, et al. (1999) Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation. Science 283:987-990.
    • (1999) Science , vol.283 , pp. 987-990
    • Livnah, O.1
  • 22
    • 0033574713 scopus 로고    scopus 로고
    • Crystal structure of the interleukin-4/receptor α chain complex reveals a mosaic binding interface
    • Hage T, Sebald W, Reinemer P (1999) Crystal structure of the interleukin-4/receptor αchain complex reveals a mosaic binding interface. Cell 97:271-281. (Pubitemid 29194277)
    • (1999) Cell , vol.97 , Issue.2 , pp. 271-281
    • Hage, T.1    Sebald, W.2    Reinemer, P.3
  • 23
  • 24
    • 34848820556 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction of human interleukin-7 bound to unglycosylated and glycosylated forms of its α-receptor
    • Wickham J, Jr., Walsh ST (2007) Crystallization and preliminary X-ray diffraction of human interleukin-7 bound to unglycosylated and glycosylated forms of its α-receptor. Acta Crystallogr Sect F Struct Biol Cryst Commun 63:865-869.
    • (2007) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.63 , pp. 865-869
    • Wickham Jr., J.1    Walsh, S.T.2
  • 26
    • 0038265184 scopus 로고    scopus 로고
    • 2 receptor
    • DOI 10.1074/jbc.M301757200
    • Rose T, Moreau JL, Eckenberg R, Thèze J (2003) Structural analysis and modeling of a synthetic interleukin-2 mimetic and its interleukin-2Rβ2 receptor. J Biol Chem 278: 22868-22876. (Pubitemid 36830350)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.25 , pp. 22868-22876
    • Rose, T.1    Moreau, J.-L.2    Eckenberg, R.3    Theze, J.4
  • 27
    • 55749094535 scopus 로고    scopus 로고
    • Human IL-Rβ chains form IL-2 binding homodimers
    • Pillet AH, et al. (2008) Human IL-Rβ chains form IL-2 binding homodimers. Eur Cytokine Netw 19(1):49-59.
    • (2008) Eur Cytokine Netw , vol.19 , Issue.1 , pp. 49-59
    • Pillet, A.H.1
  • 29
    • 33644540157 scopus 로고    scopus 로고
    • Crystal structure of the IL-2 signaling complex: Paradigm for a heterotrimeric cytokine receptor
    • Stauber DJ, et al. (2006) Crystal structure of the IL-2 signaling complex: Paradigm for a heterotrimeric cytokine receptor. Proc Natl Acad Sci USA 103:2788-2793.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2788-2793
    • Stauber, D.J.1
  • 31
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy I, Wilson IA, Michnick SW (1999) Erythropoietin receptor activation by a ligand-induced conformation change. Science 283:990-993.
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1    Wilson, I.A.2    Michnick, S.W.3
  • 32
    • 79956108320 scopus 로고    scopus 로고
    • Gain-of-function mutations in interleukin-7 receptor-α (IL7R) in childhood acute lymphoblastic leukemias
    • Shochat C, et al. (2011) Gain-of-function mutations in interleukin-7 receptor-α (IL7R) in childhood acute lymphoblastic leukemias. J Exp Med 208:901-908.
    • (2011) J Exp Med , vol.208 , pp. 901-908
    • Shochat, C.1
  • 33
    • 33846399142 scopus 로고    scopus 로고
    • z, a Depth-dependent Potential for Assessing the Energies of Insertion of Amino Acid Side-chains into Membranes: Derivation and Applications to Determining the Orientation of Transmembrane and Interfacial Helices
    • DOI 10.1016/j.jmb.2006.09.020, PII S0022283606012095
    • Senes A, et al. (2007) E(z), a depth-dependent potential for assessing the energies of insertion of amino acid side-chains into membranes: Derivation and applications to determining the orientation of transmembrane and interfacial helices. J Mol Biol 366: 436-448. (Pubitemid 46136195)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.2 , pp. 436-448
    • Senes, A.1    Chadi, D.C.2    Law, P.B.3    Walters, R.F.S.4    Nanda, V.5    DeGrado, W.F.6
  • 34
    • 76249096219 scopus 로고    scopus 로고
    • Functional screening identifies CRLF2 in precursor B-cell acute lymphoblastic leukemia
    • Yoda A, et al. (2010) Functional screening identifies CRLF2 in precursor B-cell acute lymphoblastic leukemia. Proc Natl Acad Sci USA 107:252-257.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 252-257
    • Yoda, A.1
  • 36
    • 33646381647 scopus 로고    scopus 로고
    • Active conformation of the erythropoietin receptor: Random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains
    • DOI 10.1074/jbc.M512638200
    • Lu X, Gross AW, Lodish HF (2006) Active conformation of the erythropoietin receptor: Random and cysteine-scanning mutagenesis of the extracellular juxtamembrane and transmembrane domains. J Biol Chem 281:7002-7011. (Pubitemid 43847463)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.11 , pp. 7002-7011
    • Lu, X.1    Gross, A.W.2    Lodish, H.F.3
  • 37
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon MA, Schlessinger J (2010) Cell signaling by receptor tyrosine kinases. Cell 141:1117-1134.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 38
    • 0030041323 scopus 로고    scopus 로고
    • Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: One high-affinity and one low-affinity interaction
    • DOI 10.1021/bi9524272
    • Philo JS, Aoki KH, Arakawa T, Narhi LO, Wen J (1996) Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: One high-affinity and one lowaffinity interaction. Biochemistry 35:1681-1691. (Pubitemid 26055303)
    • (1996) Biochemistry , vol.35 , Issue.5 , pp. 1681-1691
    • Philo, J.S.1    Aoki, K.H.2    Arakawa, T.3    Narhi, L.O.4    Wen, J.5
  • 40
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 54: 905-921.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , pp. 905-921
    • Brünger, A.T.1


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