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Volumn 467, Issue 7319, 2010, Pages 1118-1122

Structural basis of semaphoring-plexin signalling

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; MUTANT PROTEIN; PLEXIN; PLEXIN A2; PLEXIN B1; SEMAPHORIN; SEMAPHORIN 4D; SEMAPHORIN 6A; UNCLASSIFIED DRUG; CD100 ANTIGEN; CELL ADHESION MOLECULE; CELL SURFACE RECEPTOR; LEUKOCYTE ANTIGEN; LIGAND; NERVE PROTEIN; PLXNA2 PROTEIN, MOUSE; PLXNB1 PROTEIN, HUMAN; SEMA6A PROTEIN, MOUSE;

EID: 78049406651     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09468     Document Type: Article
Times cited : (197)

References (52)
  • 2
    • 20244364929 scopus 로고    scopus 로고
    • Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates
    • Tamagnone, L. et al. Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates. Cell 99, 71-80 (1999).
    • (1999) Cell , vol.99 , pp. 71-80
    • Tamagnone, L.1
  • 3
    • 33846813790 scopus 로고    scopus 로고
    • Interactions between plexin-A2, plexin-A4, and semaphorin 6A control lamina-restricted projection of hippocampal mossy fibers
    • Suto, F. et al. Interactions between plexin-A2, plexin-A4, and semaphorin 6A control lamina-restricted projection of hippocampal mossy fibers. Neuron 53, 535-547 (2007).
    • (2007) Neuron , vol.53 , pp. 535-547
    • Suto, F.1
  • 4
    • 0027787683 scopus 로고
    • The semaphorin genes encode a family oftransmembrane and secreted growth cone guidance molecules
    • Kolodkin, A. L., Matthes, D. J. & Goodman, C. S. The semaphorin genes encode a family oftransmembrane and secreted growth cone guidance molecules. Cell 75, 1389-1399 (1993).
    • (1993) Cell , vol.75 , pp. 1389-1399
    • Kolodkin, A.L.1    Matthes, D.J.2    Goodman, C.S.3
  • 5
    • 0141507038 scopus 로고    scopus 로고
    • The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D
    • Love, C. A. et al. The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D. Nature Struct. Biol. 10, 843-848 (2003).
    • (2003) Nature Struct. Biol. , vol.10 , pp. 843-848
    • Love, C.A.1
  • 6
    • 0041520529 scopus 로고    scopus 로고
    • Structure of the semaphorin-3A receptor binding module
    • Antipenko, A. et al. Structure of the semaphorin-3A receptor binding module. Neuron 39, 589-598 (2003).
    • (2003) Neuron , vol.39 , pp. 589-598
    • Antipenko, A.1
  • 7
    • 0032433853 scopus 로고    scopus 로고
    • Plexin A is a neuronal semaphorin receptor that controls axon guidance
    • Winberg, M. L. et al. Plexin A is a neuronal semaphorin receptor that controls axon guidance. Cell 95, 903-916 (1998).
    • (1998) Cell , vol.95 , pp. 903-916
    • Winberg, M.L.1
  • 8
    • 69449097679 scopus 로고    scopus 로고
    • Semaphorinsignalingincancer cells andincells of the tumor microenvironment-two sides of a coin
    • Capparuccia, L.&Tamagnone, L.Semaphorinsignalingincancer cells andincells of the tumor microenvironment-two sides of a coin. J. Cell Sci. 122, 1723-1736 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 1723-1736
    • Capparuccia, L.1    Tamagnone, L.2
  • 9
    • 58149240678 scopus 로고    scopus 로고
    • A functional role for semaphorin 4D/plexin B1 interactions in epithelial branching morphogenesis during organogenesis
    • Korostylev, A. et al. A functional role for semaphorin 4D/plexin B1 interactions in epithelial branching morphogenesis during organogenesis. Development 135, 3333-3343 (2008).
    • (2008) Development , vol.135 , pp. 3333-3343
    • Korostylev, A.1
  • 10
    • 27644454002 scopus 로고    scopus 로고
    • The transmembrane semaphorin Sema6A controls cerebellar granule cell migration
    • Kerjan, G. et al. The transmembrane semaphorin Sema6A controls cerebellar granule cell migration. Nature Neurosci. 8, 1516-1524 (2005).
    • (2005) Nature Neurosci. , vol.8 , pp. 1516-1524
    • Kerjan, G.1
  • 11
    • 41249099068 scopus 로고    scopus 로고
    • Plexin-A2 and its ligand, Sema6A, control nucleus-centrosome coupling in migrating granule cells
    • Renaud, J. et al. Plexin-A2 and its ligand, Sema6A, control nucleus-centrosome coupling in migrating granule cells. Nature Neurosci. 11, 440-449 (2008).
    • (2008) Nature Neurosci. , vol.11 , pp. 440-449
    • Renaud, J.1
  • 12
    • 70349453563 scopus 로고    scopus 로고
    • Crystal structure of the plexin A3 intracellular region reveals an autoinhibited conformation through active site sequestration
    • He, H., Yang, T., Terman, J. R. & Zhang, X. Crystal structure of the plexin A3 intracellular region reveals an autoinhibited conformation through active site sequestration. Proc. Natl Acad. Sci. USA 106, 15610-15615 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 15610-15615
    • He, H.1    Yang, T.2    Terman, J.R.3    Zhang, X.4
  • 13
    • 72149087958 scopus 로고    scopus 로고
    • Structure and function of the intracellular region of the plexin-B1 transmembrane receptor
    • Tong, Y. et al. Structure and function of the intracellular region of the plexin-B1 transmembrane receptor. J. Biol. Chem. 284, 35962-35972 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 35962-35972
    • Tong, Y.1
  • 14
    • 0035105491 scopus 로고    scopus 로고
    • Plexina1 autoinhibition by the plexin sema domain
    • Takahashi, T. & Strittmatter, S. M. Plexina1 autoinhibition by the plexin sema domain. Neuron 29, 429-439 (2001).
    • (2001) Neuron , vol.29 , pp. 429-439
    • Takahashi, T.1    Strittmatter, S.M.2
  • 15
    • 0033214312 scopus 로고    scopus 로고
    • Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors
    • Takahashi, T. et al. Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors. Cell 99, 59-69 (1999).
    • (1999) Cell , vol.99 , pp. 59-69
    • Takahashi, T.1
  • 16
    • 10644250013 scopus 로고    scopus 로고
    • Molecular dissection of the semaphorin 4D receptor plexin-B1-stimulated R-Ras GTPase-activating protein activity and neurite remodeling in hippocampal neurons
    • Oinuma, I., Katoh, H. & Negishi, M. Molecular dissection of the semaphorin 4D receptor plexin-B1-stimulated R-Ras GTPase-activating protein activity and neurite remodeling in hippocampal neurons. J. Neurosci. 24, 11473-11480 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 11473-11480
    • Oinuma, I.1    Katoh, H.2    Negishi, M.3
  • 17
    • 37549021146 scopus 로고    scopus 로고
    • Binding of Rac1, Rnd1, and RhoD toa novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain
    • Tong, Y. et al. Binding of Rac1, Rnd1, and RhoD toa novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain. J. Biol. Chem. 282, 37215-37224 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 37215-37224
    • Tong, Y.1
  • 19
    • 3142595278 scopus 로고    scopus 로고
    • Crystal structure of the HGF b-chain in complex with the Sema domain of the Met receptor
    • Stamos, J., Lazarus, R.A., Yao, X., Kirchhofer, D. & Wiesmann, C.Crystal structure of the HGF b-chain in complex with the Sema domain of the Met receptor. EMBO J. 23, 2325-2335 (2004).
    • (2004) EMBO J. , vol.23 , pp. 2325-2335
    • Stamos, J.1    Lazarus, R.A.2    Yao, X.3    Kirchhofer, D.4    Wiesmann, C.5
  • 20
    • 34447548559 scopus 로고    scopus 로고
    • Structure of the human receptor tyrosine kinase met in complex with the Listeria invasion protein InlB
    • Niemann, H. H. et al. Structure of the human receptor tyrosine kinase met in complex with the Listeria invasion protein InlB. Cell 130, 235-246 (2007).
    • (2007) Cell , vol.130 , pp. 235-246
    • Niemann, H.H.1
  • 21
    • 0030886550 scopus 로고    scopus 로고
    • A 70 amino acid region within the semaphorin domain activates specific cellular responseof semaphorin family members
    • Koppel, A. M., Feiner, L., Kobayashi, H. & Raper, J. A. A 70 amino acid region within the semaphorin domain activates specific cellular responseof semaphorin family members. Neuron 19, 531-537 (1997).
    • (1997) Neuron , vol.19 , pp. 531-537
    • Koppel, A.M.1    Feiner, L.2    Kobayashi, H.3    Raper, J.A.4
  • 22
    • 0032571382 scopus 로고    scopus 로고
    • The chemorepulsive activity of the axonal guidance signal semaphorin D requires dimerization
    • Klostermann, A., Lohrum, M., Adams, R. H. & Puschel, A. W. The chemorepulsive activity of the axonal guidance signal semaphorin D requires dimerization. J. Biol. Chem. 273, 7326-7331 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 7326-7331
    • Klostermann, A.1    Lohrum, M.2    Adams, R.H.3    Puschel, A.W.4
  • 23
    • 0032546965 scopus 로고    scopus 로고
    • Collapsin-1 covalently dimerizes, and dimerization is necessary for collapsing activity
    • Koppel, A. M. & Raper, J. A. Collapsin-1 covalently dimerizes, and dimerization is necessary for collapsing activity. J. Biol. Chem. 273, 15708-15713 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 15708-15713
    • Koppel, A.M.1    Raper, J.A.2
  • 24
    • 32144457047 scopus 로고    scopus 로고
    • Plexin-induced collapse assay inCOS cells
    • Turner, L.J.& Hall, A. Plexin-induced collapse assay inCOS cells. Methods Enzymol. 406, 665-676 (2006).
    • (2006) Methods Enzymol. , vol.406 , pp. 665-676
    • Turner, L.J.1    Hall, A.2
  • 25
    • 77951619146 scopus 로고    scopus 로고
    • A forward genetic screen in mice identifies Sema3A(K108N), which binds to neuropilin-1 but cannot signal
    • Merte, J. et al. A forward genetic screen in mice identifies Sema3A(K108N), which binds to neuropilin-1 but cannot signal. J. Neurosci. 30, 5767-5775 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 5767-5775
    • Merte, J.1
  • 26
    • 77956216424 scopus 로고    scopus 로고
    • Structural basis of Semaphorin-Plexin recognition and viral mimicry from Sema7A and A39R complexes with PlexinC1
    • Liu, H. et al. Structural basis of Semaphorin-Plexin recognition and viral mimicry from Sema7A and A39R complexes with PlexinC1. Cell 142, 749-761 (2010).
    • (2010) Cell , vol.142 , pp. 749-761
    • Liu, H.1
  • 27
    • 28044451085 scopus 로고    scopus 로고
    • FARP2 triggers signals for Sema3A-mediated axonal repulsion
    • Toyofuku, T. et al. FARP2 triggers signals for Sema3A-mediated axonal repulsion. Nature Neurosci. 8, 1712-1719 (2005).
    • (2005) Nature Neurosci. , vol.8 , pp. 1712-1719
    • Toyofuku, T.1
  • 28
    • 33645235265 scopus 로고    scopus 로고
    • Structural basis of hepatocyte growth factor/scatter factor and MET signalling
    • Gherardi, E. et al. Structural basis of hepatocyte growth factor/scatter factor and MET signalling. Proc. Natl Acad. Sci. USA 103, 4046-4051 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4046-4051
    • Gherardi, E.1
  • 29
    • 33745912405 scopus 로고    scopus 로고
    • A time-and cost-efficient system for high-level protein production inmammalian cells
    • Aricescu, A. R., Lu, W. & Jones, E. Y. A time-and cost-efficient system for high-level protein production inmammalian cells. Acta Crystallogr.D62, 1243-1250 (2006).
    • (2006) Acta Crystallogr. , vol.D62 , pp. 1243-1250
    • Aricescu, A.R.1    Lu, W.2    Jones, E.Y.3
  • 30
    • 33847653747 scopus 로고    scopus 로고
    • Glycoprotein structural genomics: Solving the glycosylation problem
    • Chang, V. T. et al. Glycoprotein structural genomics: solving the glycosylation problem. Structure 15, 267-273 (2007).
    • (2007) Structure , vol.15 , pp. 267-273
    • Chang, V.T.1
  • 31
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves, P.J., Callewaert, N., Contreras, R.& Khorana, H.G. Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N- acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl Acad. Sci. USA 99, 13419-13424 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 32
    • 23844515485 scopus 로고    scopus 로고
    • A procedure for setting up high-throughput nanolitre crystallization experiments.Crystallization workflowfor initial screening, automated storage, imaging and optimization
    • Walter, T. S. et al. A procedure for setting up high-throughput nanolitre crystallization experiments.Crystallization workflowfor initial screening, automated storage, imaging and optimization. Acta Crystallogr. D 61, 651-657 (2005).
    • (2005) Acta Crystallogr. D , vol.61 , pp. 651-657
    • Walter, T.S.1
  • 33
    • 13844266400 scopus 로고    scopus 로고
    • Benefits of automated crystallization plate tracking, imaging, and analysis
    • Mayo, C. J. et al. Benefits of automated crystallization plate tracking, imaging, and analysis. Structure 13, 175-182 (2005).
    • (2005) Structure , vol.13 , pp. 175-182
    • Mayo, C.J.1
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing X-ray diffraction data collectedin oscillation mode
    • Otwinowski, Z. & Minor, W.Processing X-ray diffraction data collectedin oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans, P. Scaling and assessment of data quality. Acta Crystallogr. D 62, 72-82 (2006).
    • (2006) Acta Crystallogr. D , vol.62 , pp. 72-82
    • Evans, P.1
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for proteincrystallography
    • CCP4.
    • CCP4. The CCP4 suite: programs for proteincrystallography. Acta Crystallogr.D 50, 760-763 (1994).
    • (1994) Acta Crystallogr.D , vol.50 , pp. 760-763
  • 38
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Cryst. 40, 658-674 (2007).
    • (2007) J. Appl. Cryst. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 39
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams, P. D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948-1954 (2002).
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 40
    • 0032964481 scopus 로고    scopus 로고
    • Automatedproteinmodelbuildingcombined with iterative structure refinement
    • Perrakis, A., Morris, R.&Lamzin, V.S. Automatedproteinmodelbuildingcombined with iterative structure refinement. Nature Struct. Biol. 6, 458-463 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 41
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 42
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan, K. The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D 62, 1002-1011 (2006).
    • (2006) Acta Crystallogr. D , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 43
    • 14844321328 scopus 로고    scopus 로고
    • Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT
    • Blanc, E. et al. Refinement of severely incomplete structures with maximum likelihood in BUSTER-TNT. Acta Crystallogr. D 60, 2210-2221 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2210-2221
    • Blanc, E.1
  • 44
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis, I. W. et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375-W383 (2007).
    • (2007) Nucleic Acids Res. , vol.35
    • Davis, I.W.1
  • 45
    • 0018792428 scopus 로고
    • Crystal structure of cat ? muscle pyruvate kinase at a resolution of 2.6A
    • Stuart, D. I., Levine, M., Muirhead, H. & Stammers, D. K. Crystal structure of cat ? muscle pyruvate kinase at a resolution of 2.6A. J. Mol. Biol. 134, 109-142 (1979).
    • (1979) J. Mol. Biol. , vol.134 , pp. 109-142
    • Stuart, D.I.1    Levine, M.2    Muirhead, H.3    Stammers, D.K.4
  • 46
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N. A., Sept, D., Joseph, S., Holst, M. J. & McCammon, J. A. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl Acad. Sci. USA 98, 10037-10041 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 47
    • 36448991500 scopus 로고    scopus 로고
    • Clustal W and Clustal X version 2.0
    • Larkin, M. A. et al. Clustal W and Clustal X version 2.0. Bioinformatics 23, 2947-2948 (2007).
    • (2007) Bioinformatics , vol.23 , pp. 2947-2948
    • Larkin, M.A.1
  • 48
    • 34548232365 scopus 로고    scopus 로고
    • Inference ofmacromolecular assemblies from crystalline state
    • Krissinel, E.& Henrick, K. Inference ofmacromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797 (2007).
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 49
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet, P., Courcelle, E., Stuart, D. I. & Metoz, F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15, 305-308 (1999).
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 50
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: The projection of evolutionary conservation scores of residues on protein structures
    • Landau, M. et al. ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res. 33, W299-W302 (2005).
    • (2005) Nucleic Acids Res. , vol.33
    • Landau, M.1
  • 51
    • 0344393021 scopus 로고    scopus 로고
    • Quality control and protein folding in the secretory pathway
    • Trombetta, E. S. & Parodi, A. J. Quality control and protein folding in the secretory pathway. Annu. Rev. Cell Dev. Biol. 19, 649-676 (2003).
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 649-676
    • Trombetta, E.S.1    Parodi, A.J.2
  • 52
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysisof macromolecules bysedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. Size-distribution analysisof macromolecules bysedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78, 1606-1619 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1


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