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Volumn 110, Issue 36, 2013, Pages 14634-14639

Insights into Eph receptor tyrosine kinase activation from crystal structures of the EphA4 ectodomain and its complex with ephrin-A5

Author keywords

Crystallography; Phosphorylation; Protein; Transmembrane

Indexed keywords

EPHRIN A5; EPHRIN RECEPTOR; EPHRIN RECEPTOR A4; PROTEIN BINDING;

EID: 84883325814     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1311000110     Document Type: Article
Times cited : (59)

References (33)
  • 1
    • 0031922119 scopus 로고    scopus 로고
    • The ephrins and Eph receptors in neural development
    • DOI 10.1146/annurev.neuro.21.1.309
    • Flanagan JG, Vanderhaeghen P (1998) The ephrins and Eph receptors in neural development. Annu Rev Neurosci 21:309-345. (Pubitemid 28150666)
    • (1998) Annual Review of Neuroscience , vol.21 , pp. 309-345
    • Flanagan, J.G.1    Vanderhaeghen, P.2
  • 2
    • 35548948069 scopus 로고    scopus 로고
    • Cell-cell signaling via Eph receptors and ephrins
    • DOI 10.1016/j.ceb.2007.08.004, PII S0955067407001214, Cell to Cell Contact and Extracellular Matrix
    • Himanen JP, Saha N, Nikolov DB (2007) Cell-cell signaling via Eph receptors and ephrins. Curr Opin Cell Biol 19(5):534-542. (Pubitemid 350016850)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.5 , pp. 534-542
    • Himanen, J.-P.1    Saha, N.2    Nikolov, D.B.3
  • 3
    • 0035313727 scopus 로고    scopus 로고
    • Excitatory Eph receptors and adhesive ephrin ligands
    • Klein R (2001) Excitatory Eph receptors and adhesive ephrin ligands. Curr Opin Cell Biol 13(2):196-203.
    • (2001) Curr Opin Cell Biol , vol.13 , Issue.2 , pp. 196-203
    • Klein, R.1
  • 4
    • 0035855819 scopus 로고    scopus 로고
    • The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals
    • DOI 10.1038/35093123
    • Cowan CA, Henkemeyer M (2001) The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals. Nature 413(6852):174-179. (Pubitemid 32867879)
    • (2001) Nature , vol.413 , Issue.6852 , pp. 174-179
    • Cowan, C.A.1    Henkemeyer, M.2
  • 5
    • 11144354644 scopus 로고    scopus 로고
    • Repelling class discrimination: Ephrin-A5 binds to and activates EphB2 receptor signaling
    • Himanen JP, et al. (2004) Repelling class discrimination: Ephrin-A5 binds to and activates EphB2 receptor signaling. Nat Neurosci 7(5):501-509.
    • (2004) Nat Neurosci , vol.7 , Issue.5 , pp. 501-509
    • Himanen, J.P.1
  • 6
    • 0031213749 scopus 로고    scopus 로고
    • The EphA4 and EphB1 receptor tyrosine kinases and ephrin-B2 ligand regulate targeted of branchial neural crest cells
    • Smith A, Robinson V, Patel K, Wilkinson DG (1997) The EphA4 and EphB1 receptor tyrosine kinases and ephrin-B2 ligand regulate targeted migration of branchial neural crest cells. Curr Biol 7(8):561-570. (Pubitemid 27335651)
    • (1997) Current Biology , vol.7 , Issue.8 , pp. 561-570
    • Smith, A.1    Robinson, V.2    Patel, K.3    Wilkinson, D.G.4
  • 8
    • 77956262547 scopus 로고    scopus 로고
    • Crystal structure of the ligand-binding domain of the promiscuous EphA4 receptor reveals two distinct conformations
    • Singla N, et al. (2010) Crystal structure of the ligand-binding domain of the promiscuous EphA4 receptor reveals two distinct conformations. Biochem Biophys Res Commun 399(4):555-559.
    • (2010) Biochem Biophys Res Commun , vol.399 , Issue.4 , pp. 555-559
    • Singla, N.1
  • 9
    • 41149084179 scopus 로고    scopus 로고
    • Eph-ephrin bidirectional signaling in physiology and disease
    • Pasquale EB (2008) Eph-ephrin bidirectional signaling in physiology and disease. Cell 133(1):38-52.
    • (2008) Cell , vol.133 , Issue.1 , pp. 38-52
    • Pasquale, E.B.1
  • 11
    • 10844277420 scopus 로고    scopus 로고
    • Immunocompetent mouse model of breast cancer for preclinical testing of EphA2-targeted therapy
    • DOI 10.1038/sj.cgt.7700763
    • Noblitt LW, Bangari DS, Shukla S, Mohammed S, Mittal SK (2005) Immunocompetent mouse model of breast cancer for preclinical testing of EphA2-targeted therapy. Cancer Gene Ther 12(1):46-53. (Pubitemid 39665242)
    • (2005) Cancer Gene Therapy , vol.12 , Issue.1 , pp. 46-53
    • Noblitt, L.W.1    Bangari, D.S.2    Shukla, S.3    Mohammed, S.4    Mittal, S.K.5
  • 14
    • 67650079305 scopus 로고    scopus 로고
    • Ligand recognition by A-class Eph receptors: Crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex
    • Himanen JP, et al. (2009) Ligand recognition by A-class Eph receptors: Crystal structures of the EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex. EMBO Rep 10(7):722-728.
    • (2009) EMBO Rep , vol.10 , Issue.7 , pp. 722-728
    • Himanen, J.P.1
  • 15
    • 0035924322 scopus 로고    scopus 로고
    • Crystal structure of an Eph receptor-ephrin complex
    • Himanen JP, et al. (2001) Crystal structure of an Eph receptor-ephrin complex. Nature 414(6866):933-938.
    • (2001) Nature , vol.414 , Issue.6866 , pp. 933-938
    • Himanen, J.P.1
  • 16
    • 70349774556 scopus 로고    scopus 로고
    • Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling
    • Bowden TA, et al. (2009) Structural plasticity of eph receptor A4 facilitates cross-class ephrin signaling. Structure 17(10):1386-1397.
    • (2009) Structure , vol.17 , Issue.10 , pp. 1386-1397
    • Bowden, T.A.1
  • 17
    • 57649186979 scopus 로고    scopus 로고
    • Crystal structure and NMR binding reveal that two small molecule antagonists target the high affinity ephrin-binding channel of the EphA4 receptor
    • Qin H, Shi J, Noberini R, Pasquale EB, Song J (2008) Crystal structure and NMR binding reveal that two small molecule antagonists target the high affinity ephrin-binding channel of the EphA4 receptor. J Biol Chem 283(43):29473-29484.
    • (2008) J Biol Chem , vol.283 , Issue.43 , pp. 29473-29484
    • Qin, H.1    Shi, J.2    Noberini, R.3    Pasquale, E.B.4    Song, J.5
  • 18
    • 73649128536 scopus 로고    scopus 로고
    • Structural characterization of the EphA4-Ephrin-B2 complex reveals new features enabling Eph-ephrin binding promiscuity
    • Qin H, et al. (2010) Structural characterization of the EphA4-Ephrin-B2 complex reveals new features enabling Eph-ephrin binding promiscuity. J Biol Chem 285(1):644-654.
    • (2010) J Biol Chem , vol.285 , Issue.1 , pp. 644-654
    • Qin, H.1
  • 19
    • 77954627688 scopus 로고    scopus 로고
    • Architecture of Eph receptor clusters
    • Himanen JP, et al. (2010) Architecture of Eph receptor clusters. Proc Natl Acad Sci USA 107(24):10860-10865.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.24 , pp. 10860-10865
    • Himanen, J.P.1
  • 20
    • 77950516909 scopus 로고    scopus 로고
    • An extracellular steric seeding mechanism for Eph-ephrin signaling platform assembly
    • Seiradake E, Harlos K, Sutton G, Aricescu AR, Jones EY (2010) An extracellular steric seeding mechanism for Eph-ephrin signaling platform assembly. Nat Struct Mol Biol 17(4):398-402.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.4 , pp. 398-402
    • Seiradake, E.1    Harlos, K.2    Sutton, G.3    Aricescu, A.R.4    Jones, E.Y.5
  • 21
    • 1442358805 scopus 로고    scopus 로고
    • Recruitment of Eph receptors into signaling clusters does not require ephrin contact
    • DOI 10.1083/jcb.200312001
    • Wimmer-Kleikamp SH, Janes PW, Squire A, Bastiaens PI, Lackmann M (2004) Recruitment of Eph receptors into signaling clusters does not require ephrin contact. J Cell Biol 164(5):661-666. (Pubitemid 38282950)
    • (2004) Journal of Cell Biology , vol.164 , Issue.5 , pp. 661-666
    • Wimmer-Kleikamp, S.H.1    Janes, P.W.2    Squire, A.3    Bastiaens, P.I.H.4    Lakmann, M.5
  • 22
    • 84857441823 scopus 로고    scopus 로고
    • Concepts and consequences of Eph receptor clustering
    • Janes PW, Nievergall E, Lackmann M (2012) Concepts and consequences of Eph receptor clustering. Semin Cell Dev Biol 23(1):43-50.
    • (2012) Semin Cell Dev Biol , vol.23 , Issue.1 , pp. 43-50
    • Janes, P.W.1    Nievergall, E.2    Lackmann, M.3
  • 23
    • 84855494260 scopus 로고    scopus 로고
    • Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors
    • Janes PW, et al. (2011) Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors. J Cell Biol 195(6):1033-1045.
    • (2011) J Cell Biol , vol.195 , Issue.6 , pp. 1033-1045
    • Janes, P.W.1
  • 24
    • 70249086591 scopus 로고    scopus 로고
    • Ephrin-independent regulation of cell substrate adhesion by the EphB4 receptor
    • Noren NK, Yang NY, Silldorff M, Mutyala R, Pasquale EB (2009) Ephrin-independent regulation of cell substrate adhesion by the EphB4 receptor. Biochem J 422(3):433-442.
    • (2009) Biochem J , vol.422 , Issue.3 , pp. 433-442
    • Noren, N.K.1    Yang, N.Y.2    Silldorff, M.3    Mutyala, R.4    Pasquale, E.B.5
  • 25
    • 17044377138 scopus 로고    scopus 로고
    • Coexpressed EphA receptors and ephrin-A ligands mediate opposing actions on growth cone navigation from distinct membrane domains
    • Marquardt T, et al. (2005) Coexpressed EphA receptors and ephrin-A ligands mediate opposing actions on growth cone navigation from distinct membrane domains. Cell 121(1):127-139.
    • (2005) Cell , vol.121 , Issue.1 , pp. 127-139
    • Marquardt, T.1
  • 26
    • 1242316215 scopus 로고    scopus 로고
    • EphA receptor tyrosine kinases interact with co-expressed ephrin-A ligands in cis
    • DOI 10.1016/j.neures.2003.11.009
    • Yin Y, et al. (2004) EphA receptor tyrosine kinases interact with co-expressed ephrin-A ligands in cis. Neurosci Res 48(3):285-296. (Pubitemid 38220946)
    • (2004) Neuroscience Research , vol.48 , Issue.3 , pp. 285-296
    • Yin, Y.1    Yamashita, Y.2    Noda, H.3    Okafuji, T.4    Go, M.J.5    Tanaka, H.6
  • 28
    • 79960153609 scopus 로고    scopus 로고
    • Ephrin-mediated cis-attenuation of Eph receptor signaling is essential for spinal motor axon guidance
    • Kao TJ, Kania A (2011) Ephrin-mediated cis-attenuation of Eph receptor signaling is essential for spinal motor axon guidance. Neuron 71(1):76-91.
    • (2011) Neuron , vol.71 , Issue.1 , pp. 76-91
    • Kao, T.J.1    Kania, A.2
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 2 , pp. 213-221
    • Adams, P.D.1
  • 32
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PART 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


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