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Volumn 109, Issue 9, 2015, Pages 1937-1945

Class A Plexins Are Organized as Preformed Inactive Dimers on the Cell Surface

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; NERVE PROTEIN; PHOTOPROTEIN; PLXNA4 PROTEIN, MOUSE; SEMAPHORIN;

EID: 84947547293     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2015.04.043     Document Type: Article
Times cited : (20)

References (40)
  • 1
    • 20244364929 scopus 로고    scopus 로고
    • Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates
    • L. Tamagnone, and S. Artigiani P.M. Comoglio Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates Cell 99 1999 71 80
    • (1999) Cell , vol.99 , pp. 71-80
    • Tamagnone, L.1    Artigiani, S.2    Comoglio, P.M.3
  • 2
    • 84855486320 scopus 로고    scopus 로고
    • Semaphorin signaling in angiogenesis, lymphangiogenesis and cancer
    • (Erratum in Cell Res. 2012. 22:441
    • A. Sakurai, C.L. Doçi, and J.S. Gutkind Semaphorin signaling in angiogenesis, lymphangiogenesis and cancer Cell Res. 22 2012 23 32 (Erratum in Cell Res. 2012. 22:441
    • (2012) Cell Res. , vol.22 , pp. 23-32
    • Sakurai, A.1    Doçi, C.L.2    Gutkind, J.S.3
  • 3
    • 84857686973 scopus 로고    scopus 로고
    • Diverse roles for semaphorin-plexin signaling in the immune system
    • H. Takamatsu, and A. Kumanogoh Diverse roles for semaphorin-plexin signaling in the immune system Trends Immunol. 33 2012 127 135
    • (2012) Trends Immunol. , vol.33 , pp. 127-135
    • Takamatsu, H.1    Kumanogoh, A.2
  • 4
    • 84875630392 scopus 로고    scopus 로고
    • Semaphorins in bone development, homeostasis, and disease
    • S. Kang, and A. Kumanogoh Semaphorins in bone development, homeostasis, and disease Semin. Cell Dev. Biol. 24 2013 163 171
    • (2013) Semin. Cell Dev. Biol. , vol.24 , pp. 163-171
    • Kang, S.1    Kumanogoh, A.2
  • 5
    • 84877138671 scopus 로고    scopus 로고
    • The role of semaphorins and their receptors in vascular development and cancer
    • C. Gu, and E. Giraudo The role of semaphorins and their receptors in vascular development and cancer Exp. Cell Res. 319 2013 1306 1316
    • (2013) Exp. Cell Res. , vol.319 , pp. 1306-1316
    • Gu, C.1    Giraudo, E.2
  • 6
    • 34547745841 scopus 로고    scopus 로고
    • Navigating their way to the clinic: Emerging roles for axon guidance molecules in neurological disorders and injury
    • A. Yaron, and B. Zheng Navigating their way to the clinic: emerging roles for axon guidance molecules in neurological disorders and injury Dev. Neurobiol. 67 2007 1216 1231
    • (2007) Dev. Neurobiol. , vol.67 , pp. 1216-1231
    • Yaron, A.1    Zheng, B.2
  • 7
    • 84865137629 scopus 로고    scopus 로고
    • Emerging role of semaphorins as major regulatory signals and potential therapeutic targets in cancer
    • L. Tamagnone Emerging role of semaphorins as major regulatory signals and potential therapeutic targets in cancer Cancer Cell 22 2012 145 152
    • (2012) Cancer Cell , vol.22 , pp. 145-152
    • Tamagnone, L.1
  • 10
    • 78049370988 scopus 로고    scopus 로고
    • Structural basis for semaphorin signalling through the plexin receptor
    • T. Nogi, and N. Yasui J. Takagi Structural basis for semaphorin signalling through the plexin receptor Nature 467 2010 1123 1127
    • (2010) Nature , vol.467 , pp. 1123-1127
    • Nogi, T.1    Yasui, N.2    Takagi, J.3
  • 11
    • 77956216424 scopus 로고    scopus 로고
    • Structural basis of semaphorin-plexin recognition and viral mimicry from Sema7A and A39R complexes with PlexinC1
    • H. Liu, and Z.S. Juo X. He Structural basis of semaphorin-plexin recognition and viral mimicry from Sema7A and A39R complexes with PlexinC1 Cell 142 2010 749 761
    • (2010) Cell , vol.142 , pp. 749-761
    • Liu, H.1    Juo, Z.S.2    He, X.3
  • 12
    • 78049406651 scopus 로고    scopus 로고
    • Structural basis of semaphorin-plexin signalling
    • B.J.C. Janssen, and R.A. Robinson E.Y. Jones Structural basis of semaphorin-plexin signalling Nature 467 2010 1118 1122
    • (2010) Nature , vol.467 , pp. 1118-1122
    • Janssen, B.J.C.1    Robinson, R.A.2    Jones, E.Y.3
  • 13
    • 0033214312 scopus 로고    scopus 로고
    • Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors
    • T. Takahashi, and A. Fournier S.M. Strittmatter Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors Cell 99 1999 59 69
    • (1999) Cell , vol.99 , pp. 59-69
    • Takahashi, T.1    Fournier, A.2    Strittmatter, S.M.3
  • 14
    • 84870784265 scopus 로고    scopus 로고
    • Neuropilins lock secreted semaphorins onto plexins in a ternary signaling complex
    • B.J.C. Janssen, and T. Malinauskas E.Y. Jones Neuropilins lock secreted semaphorins onto plexins in a ternary signaling complex Nat. Struct. Mol. Biol. 19 2012 1293 1299
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 1293-1299
    • Janssen, B.J.C.1    Malinauskas, T.2    Jones, E.Y.3
  • 15
    • 0041520529 scopus 로고    scopus 로고
    • Structure of the semaphorin-3A receptor binding module
    • A. Antipenko, and J.-P. Himanen D.B. Nikolov Structure of the semaphorin-3A receptor binding module Neuron 39 2003 589 598
    • (2003) Neuron , vol.39 , pp. 589-598
    • Antipenko, A.1    Himanen, J.-P.2    Nikolov, D.B.3
  • 16
    • 0141507038 scopus 로고    scopus 로고
    • The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D
    • C.A. Love, and K. Harlos R.M. Esnouf The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D Nat. Struct. Biol. 10 2003 843 848
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 843-848
    • Love, C.A.1    Harlos, K.2    Esnouf, R.M.3
  • 17
    • 84885158575 scopus 로고    scopus 로고
    • Structural basis for activation and non-canonical catalysis of the Rap GTPase activating protein domain of plexin
    • Y. Wang, and H.G. Pascoe X. Zhang Structural basis for activation and non-canonical catalysis of the Rap GTPase activating protein domain of plexin eLife 2 2013 e01279
    • (2013) ELife , vol.2 , pp. e01279
    • Wang, Y.1    Pascoe, H.G.2    Zhang, X.3
  • 18
    • 84856070985 scopus 로고    scopus 로고
    • Plexins are GTPase-activating proteins for Rap and are activated by induced dimerization
    • Y. Wang, and H. He X. Zhang Plexins are GTPase-activating proteins for Rap and are activated by induced dimerization Sci. Signal. 5 2012 ra6
    • (2012) Sci. Signal. , vol.5 , pp. ra6
    • Wang, Y.1    He, H.2    Zhang, X.3
  • 19
    • 70349453563 scopus 로고    scopus 로고
    • Crystal structure of the plexin A3 intracellular region reveals an autoinhibited conformation through active site sequestration
    • H. He, and T. Yang X. Zhang Crystal structure of the plexin A3 intracellular region reveals an autoinhibited conformation through active site sequestration Proc. Natl. Acad. Sci. USA 106 2009 15610 15615
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 15610-15615
    • He, H.1    Yang, T.2    Zhang, X.3
  • 20
    • 72149087958 scopus 로고    scopus 로고
    • Structure and function of the intracellular region of the plexin-b1 transmembrane receptor
    • Y. Tong, and P.K. Hota M. Buck Structure and function of the intracellular region of the plexin-b1 transmembrane receptor J. Biol. Chem. 284 2009 35962 35972
    • (2009) J. Biol. Chem. , vol.284 , pp. 35962-35972
    • Tong, Y.1    Hota, P.K.2    Buck, M.3
  • 21
    • 80052339290 scopus 로고    scopus 로고
    • A dual binding mode for RhoGTPases in plexin signalling
    • C.H. Bell, and A.R. Aricescu C. Siebold A dual binding mode for RhoGTPases in plexin signalling PLoS Biol. 9 2011 e1001134
    • (2011) PLoS Biol. , vol.9 , pp. e1001134
    • Bell, C.H.1    Aricescu, A.R.2    Siebold, C.3
  • 22
    • 0034550281 scopus 로고    scopus 로고
    • The semaphorin 3A receptor may directly regulate the activity of small GTPases
    • B. Rohm, and B. Rahim A.W. Püschel The semaphorin 3A receptor may directly regulate the activity of small GTPases FEBS Lett. 486 2000 68 72
    • (2000) FEBS Lett. , vol.486 , pp. 68-72
    • Rohm, B.1    Rahim, B.2    Püschel, A.W.3
  • 23
    • 79959393264 scopus 로고    scopus 로고
    • Structure-function relationships of the G domain, a canonical switch motif
    • A. Wittinghofer, and I.R. Vetter Structure-function relationships of the G domain, a canonical switch motif Annu. Rev. Biochem. 80 2011 943 971
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 943-971
    • Wittinghofer, A.1    Vetter, I.R.2
  • 24
    • 0035105491 scopus 로고    scopus 로고
    • Plexina1 autoinhibition by the plexin sema domain
    • T. Takahashi, and S.M. Strittmatter Plexina1 autoinhibition by the plexin sema domain Neuron 29 2001 429 439
    • (2001) Neuron , vol.29 , pp. 429-439
    • Takahashi, T.1    Strittmatter, S.M.2
  • 25
    • 37549021146 scopus 로고    scopus 로고
    • Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain
    • Y. Tong, and P. Chugha M. Buck Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain J. Biol. Chem. 282 2007 37215 37224
    • (2007) J. Biol. Chem. , vol.282 , pp. 37215-37224
    • Tong, Y.1    Chugha, P.2    Buck, M.3
  • 26
    • 79960432633 scopus 로고    scopus 로고
    • Structural basis of Rnd1 binding to plexin Rho GTPase binding domains (RBDs)
    • H. Wang, and P.K. Hota H.-W. Park Structural basis of Rnd1 binding to plexin Rho GTPase binding domains (RBDs) J. Biol. Chem. 286 2011 26093 26106
    • (2011) J. Biol. Chem. , vol.286 , pp. 26093-26106
    • Wang, H.1    Hota, P.K.2    Park, H.-W.3
  • 27
    • 0030895059 scopus 로고    scopus 로고
    • Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution
    • P. Schwille, F.J. Meyer-Almes, and R. Rigler Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution Biophys. J. 72 1997 1878 1886
    • (1997) Biophys. J. , vol.72 , pp. 1878-1886
    • Schwille, P.1    Meyer-Almes, F.J.2    Rigler, R.3
  • 28
    • 31744436399 scopus 로고    scopus 로고
    • Fluorescence cross-correlation spectroscopy in living cells
    • K. Bacia, S.A. Kim, and P. Schwille Fluorescence cross-correlation spectroscopy in living cells Nat. Methods 3 2006 83 89
    • (2006) Nat. Methods , vol.3 , pp. 83-89
    • Bacia, K.1    Kim, S.A.2    Schwille, P.3
  • 29
    • 68949136866 scopus 로고    scopus 로고
    • Determination of dissociation constants in living zebrafish embryos with single wavelength fluorescence cross-correlation spectroscopy
    • X. Shi, and Y.H. Foo T. Wohland Determination of dissociation constants in living zebrafish embryos with single wavelength fluorescence cross-correlation spectroscopy Biophys. J. 97 2009 678 686
    • (2009) Biophys. J. , vol.97 , pp. 678-686
    • Shi, X.1    Foo, Y.H.2    Wohland, T.3
  • 31
    • 84858040463 scopus 로고    scopus 로고
    • Factors affecting the quantification of biomolecular interactions by fluorescence cross-correlation spectroscopy
    • Y.H. Foo, and N. Naredi-Rainer T. Wohland Factors affecting the quantification of biomolecular interactions by fluorescence cross-correlation spectroscopy Biophys. J. 102 2012 1174 1183
    • (2012) Biophys. J. , vol.102 , pp. 1174-1183
    • Foo, Y.H.1    Naredi-Rainer, N.2    Wohland, T.3
  • 32
    • 84902265013 scopus 로고    scopus 로고
    • Time-resolved fluorescence spectroscopy measures clustering and mobility of a G protein-coupled receptor opsin in live cell membranes
    • W.D. Comar, and S.M. Schubert A.W. Smith Time-resolved fluorescence spectroscopy measures clustering and mobility of a G protein-coupled receptor opsin in live cell membranes J. Am. Chem. Soc. 136 2014 8342 8349
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 8342-8349
    • Comar, W.D.1    Schubert, S.M.2    Smith, A.W.3
  • 33
    • 84873280409 scopus 로고    scopus 로고
    • Conformational coupling across the plasma membrane in activation of the EGF receptor
    • N.F. Endres, and R. Das J. Kuriyan Conformational coupling across the plasma membrane in activation of the EGF receptor Cell 152 2013 543 556
    • (2013) Cell , vol.152 , pp. 543-556
    • Endres, N.F.1    Das, R.2    Kuriyan, J.3
  • 34
    • 84863524237 scopus 로고    scopus 로고
    • Monitoring lipid anchor organization in cell membranes by PIE-FCCS
    • S.B. Triffo, and H.H. Huang J.T. Groves Monitoring lipid anchor organization in cell membranes by PIE-FCCS J. Am. Chem. Soc. 134 2012 10833 10842
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 10833-10842
    • Triffo, S.B.1    Huang, H.H.2    Groves, J.T.3
  • 35
    • 84885906578 scopus 로고    scopus 로고
    • Strengths and weaknesses of recently engineered red fluorescent proteins evaluated in live cells using fluorescence correlation spectroscopy
    • A.P. Siegel, and M.A. Baird R.N. Day Strengths and weaknesses of recently engineered red fluorescent proteins evaluated in live cells using fluorescence correlation spectroscopy Int. J. Mol. Sci. 14 2013 20340 20358
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 20340-20358
    • Siegel, A.P.1    Baird, M.A.2    Day, R.N.3
  • 36
    • 84911396858 scopus 로고    scopus 로고
    • Crystal structure of a lipoxygenase in complex with substrate: The arachidonic acid binding site of 8R-lipoxygenase
    • D.B. Neau, and G. Bender M.E. Newcomer Crystal structure of a lipoxygenase in complex with substrate: the arachidonic acid binding site of 8R-lipoxygenase J. Biol. Chem. 289 2014 31905 31913
    • (2014) J. Biol. Chem. , vol.289 , pp. 31905-31913
    • Neau, D.B.1    Bender, G.2    Newcomer, M.E.3
  • 37
    • 84914142936 scopus 로고    scopus 로고
    • Emerging concepts in the regulation of the EGF receptor and other receptor tyrosine kinases
    • N.F. Endres, and T. Barros J. Kuriyan Emerging concepts in the regulation of the EGF receptor and other receptor tyrosine kinases Trends Biochem. Sci. 39 2014 437 446
    • (2014) Trends Biochem. Sci. , vol.39 , pp. 437-446
    • Endres, N.F.1    Barros, T.2    Kuriyan, J.3
  • 38
    • 34247230905 scopus 로고    scopus 로고
    • Unligated epidermal growth factor receptor forms higher order oligomers within microclusters on A431 cells that are sensitive to tyrosine kinase inhibitor binding
    • A.H.A. Clayton, M.L. Tavarnesi, and T.G. Johns Unligated epidermal growth factor receptor forms higher order oligomers within microclusters on A431 cells that are sensitive to tyrosine kinase inhibitor binding Biochemistry 46 2007 4589 4597
    • (2007) Biochemistry , vol.46 , pp. 4589-4597
    • Clayton, A.H.A.1    Tavarnesi, M.L.2    Johns, T.G.3
  • 39
    • 84920373653 scopus 로고    scopus 로고
    • How IGF-1 activates its receptor
    • J.M. Kavran, and J.M. McCabe D.J. Leahy How IGF-1 activates its receptor eLife 3 2014 e03772
    • (2014) ELife , vol.3 , pp. e03772
    • Kavran, J.M.1    McCabe, J.M.2    Leahy, D.J.3
  • 40
    • 0023156382 scopus 로고
    • Self-phosphorylation of epidermal growth factor receptor: Evidence for a model of intermolecular allosteric activation
    • Y. Yarden, and J. Schlessinger Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activation Biochemistry 26 1987 1434 1442
    • (1987) Biochemistry , vol.26 , pp. 1434-1442
    • Yarden, Y.1    Schlessinger, J.2


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