메뉴 건너뛰기




Volumn 46, Issue 2, 2005, Pages 205-217

Vav family GEFs link activated Ephs to endocytosis and axon guidance

Author keywords

[No Author keywords available]

Indexed keywords

EPHRIN; RHO FACTOR; VAV PROTEIN;

EID: 20244369288     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuron.2005.03.019     Document Type: Article
Times cited : (200)

References (66)
  • 1
    • 0034269240 scopus 로고    scopus 로고
    • Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation
    • B. Aghazadeh, W.E. Lowry, X.Y. Huang, and M.K. Rosen Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation Cell 102 2000 625 633
    • (2000) Cell , vol.102 , pp. 625-633
    • Aghazadeh, B.1    Lowry, W.E.2    Huang, X.Y.3    Rosen, M.K.4
  • 2
    • 5444230311 scopus 로고    scopus 로고
    • Rap1 promotes cell spreading by localizing Rac guanine nucleotide exchange factors
    • W.T. Arthur, L.A. Quilliam, and J.A. Cooper Rap1 promotes cell spreading by localizing Rac guanine nucleotide exchange factors J. Cell Biol. 167 2004 111 122
    • (2004) J. Cell Biol. , vol.167 , pp. 111-122
    • Arthur, W.T.1    Quilliam, L.A.2    Cooper, J.A.3
  • 4
    • 0034086061 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors
    • K.L. Binns, P.P. Taylor, F. Sicheri, T. Pawson, and S.J. Holland Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors Mol. Cell. Biol. 20 2000 4791 4805
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4791-4805
    • Binns, K.L.1    Taylor, P.P.2    Sicheri, F.3    Pawson, T.4    Holland, S.J.5
  • 5
    • 0033974061 scopus 로고    scopus 로고
    • Regulatory and signaling properties of the Vav family
    • X.R. Bustelo Regulatory and signaling properties of the Vav family Mol. Cell. Biol. 20 2000 1461 1477
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1461-1477
    • Bustelo, X.R.1
  • 6
    • 0035473464 scopus 로고    scopus 로고
    • Vav proteins, adaptors and cell signaling
    • X.R. Bustelo Vav proteins, adaptors and cell signaling Oncogene 20 2001 6372 6381
    • (2001) Oncogene , vol.20 , pp. 6372-6381
    • Bustelo, X.R.1
  • 7
    • 0037396618 scopus 로고    scopus 로고
    • Distribution of p120 catenin during rat brain development: Potential role in regulation of cadherin-mediated adhesion and actin cytoskeleton organization
    • N. Chauvet, M. Prieto, C. Fabre, N.K. Noren, and A. Privat Distribution of p120 catenin during rat brain development: potential role in regulation of cadherin-mediated adhesion and actin cytoskeleton organization Mol. Cell. Neurosci. 22 2003 467 486
    • (2003) Mol. Cell. Neurosci. , vol.22 , pp. 467-486
    • Chauvet, N.1    Prieto, M.2    Fabre, C.3    Noren, N.K.4    Privat, A.5
  • 8
    • 0031033292 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product
    • P. Crespo, K.E. Schuebel, A.A. Ostrom, J.S. Gutkind, and X.R. Bustelo Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product Nature 385 1997 169 172
    • (1997) Nature , vol.385 , pp. 169-172
    • Crespo, P.1    Schuebel, K.E.2    Ostrom, A.A.3    Gutkind, J.S.4    Bustelo, X.R.5
  • 9
    • 0028241739 scopus 로고
    • Microtubule dynamics modulated by guanosine triphosphate hydrolysis activity of beta-tubulin
    • A. Davis, C.R. Sage, C.A. Dougherty, and K.W. Farrell Microtubule dynamics modulated by guanosine triphosphate hydrolysis activity of beta-tubulin Science 264 1994 839 842
    • (1994) Science , vol.264 , pp. 839-842
    • Davis, A.1    Sage, C.R.2    Dougherty, C.A.3    Farrell, K.W.4
  • 10
    • 0037083485 scopus 로고    scopus 로고
    • Eph receptor tyrosine kinase-mediated formation of a topographic map in the Drosophila visual system
    • R. Dearborn Jr., Q. He, S. Kunes, and Y. Dai Eph receptor tyrosine kinase-mediated formation of a topographic map in the Drosophila visual system J. Neurosci. 22 2002 1338 1349
    • (2002) J. Neurosci. , vol.22 , pp. 1338-1349
    • Dearborn Jr., R.1    He, Q.2    Kunes, S.3    Dai, Y.4
  • 11
    • 0029082312 scopus 로고
    • In vitro guidance of retinal ganglion cell axons by RAGS, a 25 kDa tectal protein related to ligands for Eph receptor tyrosine kinases
    • U. Drescher, C. Kremoser, C. Handwerker, J. Loschinger, M. Noda, and F. Bonhoeffer In vitro guidance of retinal ganglion cell axons by RAGS, a 25 kDa tectal protein related to ligands for Eph receptor tyrosine kinases Cell 82 1995 359 370
    • (1995) Cell , vol.82 , pp. 359-370
    • Drescher, U.1    Kremoser, C.2    Handwerker, C.3    Loschinger, J.4    Noda, M.5    Bonhoeffer, F.6
  • 12
    • 0029867243 scopus 로고    scopus 로고
    • A juxtamembrane autophosphorylation site in the Eph family receptor tyrosine kinase, Sek, mediates high affinity interaction with p59fyn
    • C. Ellis, F. Kasmi, P. Ganju, E. Walls, G. Panayotou, and A.D. Reith A juxtamembrane autophosphorylation site in the Eph family receptor tyrosine kinase, Sek, mediates high affinity interaction with p59fyn Oncogene 12 1996 1727 1736
    • (1996) Oncogene , vol.12 , pp. 1727-1736
    • Ellis, C.1    Kasmi, F.2    Ganju, P.3    Walls, E.4    Panayotou, G.5    Reith, A.D.6
  • 14
    • 0033681554 scopus 로고    scopus 로고
    • Genetic analysis of ephrin-A2 and ephrin-A5 shows their requirement in multiple aspects of retinocollicular mapping
    • D.A. Feldheim, Y.I. Kim, A.D. Bergemann, J. Frisen, M. Barbacid, and J.G. Flanagan Genetic analysis of ephrin-A2 and ephrin-A5 shows their requirement in multiple aspects of retinocollicular mapping Neuron 25 2000 563 574
    • (2000) Neuron , vol.25 , pp. 563-574
    • Feldheim, D.A.1    Kim, Y.I.2    Bergemann, A.D.3    Frisen, J.4    Barbacid, M.5    Flanagan, J.G.6
  • 15
    • 0031922119 scopus 로고    scopus 로고
    • The ephrins and Eph receptors in neural development
    • J.G. Flanagan, and P. Vanderhaeghen The ephrins and Eph receptors in neural development Annu. Rev. Neurosci. 21 1998 309 345
    • (1998) Annu. Rev. Neurosci. , vol.21 , pp. 309-345
    • Flanagan, J.G.1    Vanderhaeghen, P.2
  • 16
    • 0034678343 scopus 로고    scopus 로고
    • Semaphorin3A enhances endocytosis at sites of receptor-F-actin colocalization during growth cone collapse
    • A.E. Fournier, F. Nakamura, S. Kawamoto, Y. Goshima, R.G. Kalb, and S.M. Strittmatter Semaphorin3A enhances endocytosis at sites of receptor-F-actin colocalization during growth cone collapse J. Cell Biol. 149 2000 411 422
    • (2000) J. Cell Biol. , vol.149 , pp. 411-422
    • Fournier, A.E.1    Nakamura, F.2    Kawamoto, S.3    Goshima, Y.4    Kalb, R.G.5    Strittmatter, S.M.6
  • 17
    • 0032006223 scopus 로고    scopus 로고
    • Ephrin-A5 (AL-1/RAGS) is essential for proper retinal axon guidance and topographic mapping in the mammalian visual system
    • J. Frisen, P.A. Yates, T. McLaughlin, G.C. Friedman, D.D. O'Leary, and M. Barbacid Ephrin-A5 (AL-1/RAGS) is essential for proper retinal axon guidance and topographic mapping in the mammalian visual system Neuron 20 1998 235 243
    • (1998) Neuron , vol.20 , pp. 235-243
    • Frisen, J.1    Yates, P.A.2    McLaughlin, T.3    Friedman, G.C.4    O'Leary, D.D.5    Barbacid, M.6
  • 18
    • 0344861826 scopus 로고    scopus 로고
    • Signalling mechanisms mediating neuronal responses to guidance cues
    • K.L. Guan, and Y. Rao Signalling mechanisms mediating neuronal responses to guidance cues Nat. Rev. Neurosci. 4 2003 941 956
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 941-956
    • Guan, K.L.1    Rao, Y.2
  • 19
    • 0034714357 scopus 로고    scopus 로고
    • Regulated cleavage of a contact-mediated axon repellent
    • M. Hattori, M. Osterfield, and J.G. Flanagan Regulated cleavage of a contact-mediated axon repellent Science 289 2000 1360 1365
    • (2000) Science , vol.289 , pp. 1360-1365
    • Hattori, M.1    Osterfield, M.2    Flanagan, J.G.3
  • 20
    • 0030847193 scopus 로고    scopus 로고
    • Neuropilin is a receptor for the axonal chemorepellent Semaphorin III
    • Z. He, and M. Tessier-Lavigne Neuropilin is a receptor for the axonal chemorepellent Semaphorin III Cell 90 1997 739 751
    • (1997) Cell , vol.90 , pp. 739-751
    • He, Z.1    Tessier-Lavigne, M.2
  • 21
    • 2542421751 scopus 로고    scopus 로고
    • Dynein motors transport activated Trks to promote survival of target-dependent neurons
    • H.M. Heerssen, M.F. Pazyra, and R.A. Segal Dynein motors transport activated Trks to promote survival of target-dependent neurons Nat. Neurosci. 7 2004 596 604
    • (2004) Nat. Neurosci. , vol.7 , pp. 596-604
    • Heerssen, H.M.1    Pazyra, M.F.2    Segal, R.A.3
  • 22
    • 0347993700 scopus 로고    scopus 로고
    • Multiple EphB receptor tyrosine kinases shape dendritic spines in the hippocampus
    • M. Henkemeyer, O.S. Itkis, M. Ngo, P.W. Hickmott, and I.M. Ethell Multiple EphB receptor tyrosine kinases shape dendritic spines in the hippocampus J. Cell Biol. 163 2003 1313 1326
    • (2003) J. Cell Biol. , vol.163 , pp. 1313-1326
    • Henkemeyer, M.1    Itkis, O.S.2    Ngo, M.3    Hickmott, P.W.4    Ethell, I.M.5
  • 24
    • 0037101649 scopus 로고    scopus 로고
    • Rac1-mediated endocytosis during ephrin-A2- and semaphorin 3A-induced growth cone collapse
    • W.M. Jurney, G. Gallo, P.C. Letourneau, and S.C. McLoon Rac1-mediated endocytosis during ephrin-A2- and semaphorin 3A-induced growth cone collapse J. Neurosci. 22 2002 6019 6028
    • (2002) J. Neurosci. , vol.22 , pp. 6019-6028
    • Jurney, W.M.1    Gallo, G.2    Letourneau, P.C.3    McLoon, S.C.4
  • 25
    • 14044273991 scopus 로고    scopus 로고
    • Vav2 as a Rac-GEF responsible for the nectin-induced, c-Src- and Cdc42-mediated activation of Rac
    • T. Kawakatsu, H. Ogita, T. Fukuhara, T. Fukuyama, Y. Minami, K. Shimizu, and Y. Takai Vav2 as a Rac-GEF responsible for the nectin-induced, c-Src- and Cdc42-mediated activation of Rac J. Biol. Chem. 280 2005 4940 4947
    • (2005) J. Biol. Chem. , vol.280 , pp. 4940-4947
    • Kawakatsu, T.1    Ogita, H.2    Fukuhara, T.3    Fukuyama, T.4    Minami, Y.5    Shimizu, K.6    Takai, Y.7
  • 26
    • 0026467112 scopus 로고
    • Fasciclin IV: Sequence, expression, and function during growth cone guidance in the grasshopper embryo
    • A.L. Kolodkin, D.J. Matthes, T.P. O'Connor, N.H. Patel, A. Admon, D. Bentley, and C.S. Goodman Fasciclin IV: sequence, expression, and function during growth cone guidance in the grasshopper embryo Neuron 9 1992 831 845
    • (1992) Neuron , vol.9 , pp. 831-845
    • Kolodkin, A.L.1    Matthes, D.J.2    O'Connor, T.P.3    Patel, N.H.4    Admon, A.5    Bentley, D.6    Goodman, C.S.7
  • 28
    • 0036303033 scopus 로고    scopus 로고
    • Mechanisms and functions of Eph and ephrin signalling
    • K. Kullander, and R. Klein Mechanisms and functions of Eph and ephrin signalling Nat. Rev. Mol. Cell Biol. 3 2002 475 486
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 475-486
    • Kullander, K.1    Klein, R.2
  • 29
    • 0035137449 scopus 로고    scopus 로고
    • Kinase-dependent and kinase-independent functions of EphA4 receptors in major axon tract formation in vivo
    • K. Kullander, N.K. Mather, F. Diella, M. Dottori, A.W. Boyd, and R. Klein Kinase-dependent and kinase-independent functions of EphA4 receptors in major axon tract formation in vivo Neuron 29 2001 73 84
    • (2001) Neuron , vol.29 , pp. 73-84
    • Kullander, K.1    Mather, N.K.2    Diella, F.3    Dottori, M.4    Boyd, A.W.5    Klein, R.6
  • 30
    • 3242698182 scopus 로고    scopus 로고
    • A neurotrophin signaling cascade coordinates sympathetic neuron development through differential control of TrkA trafficking and retrograde signaling
    • R. Kuruvilla, L.S. Zweifel, N.O. Glebova, B.E. Lonze, G. Valdez, H. Ye, and D.D. Ginty A neurotrophin signaling cascade coordinates sympathetic neuron development through differential control of TrkA trafficking and retrograde signaling Cell 118 2004 243 255
    • (2004) Cell , vol.118 , pp. 243-255
    • Kuruvilla, R.1    Zweifel, L.S.2    Glebova, N.O.3    Lonze, B.E.4    Valdez, G.5    Ye, H.6    Ginty, D.D.7
  • 32
    • 0033826334 scopus 로고    scopus 로고
    • Vav2 activates Rac1, Cdc42, and RhoA downstream from growth factor receptors but not beta1 integrins
    • B.P. Liu, and K. Burridge Vav2 activates Rac1, Cdc42, and RhoA downstream from growth factor receptors but not beta1 integrins Mol. Cell. Biol. 20 2000 7160 7169
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7160-7169
    • Liu, B.P.1    Burridge, K.2
  • 33
    • 0037894847 scopus 로고    scopus 로고
    • Tyrosine phosphorylation mediates both activation and downmodulation of the biological activity of Vav
    • M. Lopez-Lago, H. Lee, C. Cruz, N. Movilla, and X.R. Bustelo Tyrosine phosphorylation mediates both activation and downmodulation of the biological activity of Vav Mol. Cell. Biol. 20 2000 1678 1691
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1678-1691
    • Lopez-Lago, M.1    Lee, H.2    Cruz, C.3    Movilla, N.4    Bustelo, X.R.5
  • 34
    • 0027373701 scopus 로고
    • Collapsin: A protein in brain that induces the collapse and paralysis of neuronal growth cones
    • Y. Luo, D. Raible, and J.A. Raper Collapsin: a protein in brain that induces the collapse and paralysis of neuronal growth cones Cell 75 1993 217 227
    • (1993) Cell , vol.75 , pp. 217-227
    • Luo, Y.1    Raible, D.2    Raper, J.A.3
  • 35
    • 0242721443 scopus 로고    scopus 로고
    • B-type Eph receptors and ephrins induce growth cone collapse through distinct intracellular pathways
    • F. Mann, E. Miranda, C. Weinl, E. Harmer, and C.E. Holt B-type Eph receptors and ephrins induce growth cone collapse through distinct intracellular pathways J. Neurobiol. 57 2003 323 336
    • (2003) J. Neurobiol. , vol.57 , pp. 323-336
    • Mann, F.1    Miranda, E.2    Weinl, C.3    Harmer, E.4    Holt, C.E.5
  • 36
    • 0141618355 scopus 로고    scopus 로고
    • EGF receptor mediates adhesion-dependent activation of the Rac GTPase: A role for phosphatidylinositol 3-kinase and Vav2
    • N. Marcoux, and K. Vuori EGF receptor mediates adhesion-dependent activation of the Rac GTPase: a role for phosphatidylinositol 3-kinase and Vav2 Oncogene 22 2003 6100 6106
    • (2003) Oncogene , vol.22 , pp. 6100-6106
    • Marcoux, N.1    Vuori, K.2
  • 37
    • 0035833248 scopus 로고    scopus 로고
    • Vav2 is required for cell spreading
    • P.A. Marignani, and C.L. Carpenter Vav2 is required for cell spreading J. Cell Biol. 154 2001 177 186
    • (2001) J. Cell Biol. , vol.154 , pp. 177-186
    • Marignani, P.A.1    Carpenter, C.L.2
  • 38
    • 0141839882 scopus 로고    scopus 로고
    • Rac-dependent trans-endocytosis of ephrinBs regulates Eph-ephrin contact repulsion
    • D.J. Marston, S. Dickinson, and C.D. Nobes Rac-dependent trans-endocytosis of ephrinBs regulates Eph-ephrin contact repulsion Nat. Cell Biol. 5 2003 879 888
    • (2003) Nat. Cell Biol. , vol.5 , pp. 879-888
    • Marston, D.J.1    Dickinson, S.2    Nobes, C.D.3
  • 39
    • 0031057545 scopus 로고    scopus 로고
    • AL-1-induced growth cone collapse of rat cortical neurons is correlated with REK7 expression and rearrangement of the actin cytoskeleton
    • L. Meima, I.J. Kljavin, P. Moran, A. Shih, J.W. Winslow, and I.W. Caras AL-1-induced growth cone collapse of rat cortical neurons is correlated with REK7 expression and rearrangement of the actin cytoskeleton Eur. J. Neurosci. 9 1997 177 188
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 177-188
    • Meima, L.1    Kljavin, I.J.2    Moran, P.3    Shih, A.4    Winslow, J.W.5    Caras, I.W.6
  • 40
    • 0030833727 scopus 로고    scopus 로고
    • Lerk2 (ephrin-B1) is a collapsing factor for a subset of cortical growth cones and acts by a mechanism different from AL-1 (ephrin-A5)
    • L. Meima, P. Moran, W. Matthews, and I.W. Caras Lerk2 (ephrin-B1) is a collapsing factor for a subset of cortical growth cones and acts by a mechanism different from AL-1 (ephrin-A5) Mol. Cell. Neurosci. 9 1997 314 328
    • (1997) Mol. Cell. Neurosci. , vol.9 , pp. 314-328
    • Meima, L.1    Moran, P.2    Matthews, W.3    Caras, I.W.4
  • 42
    • 0032696592 scopus 로고    scopus 로고
    • Biological and regulatory properties of Vav-3, a new member of the Vav family of oncoproteins
    • N. Movilla, and X.R. Bustelo Biological and regulatory properties of Vav-3, a new member of the Vav family of oncoproteins Mol. Cell. Biol. 19 1999 7870 7885
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7870-7885
    • Movilla, N.1    Bustelo, X.R.2
  • 43
    • 0028104680 scopus 로고
    • Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity
    • A. Pandey, D.F. Lazar, A.R. Saltiel, and V.M. Dixit Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity J. Biol. Chem. 269 1994 30154 30157
    • (1994) J. Biol. Chem. , vol.269 , pp. 30154-30157
    • Pandey, A.1    Lazar, D.F.2    Saltiel, A.R.3    Dixit, V.M.4
  • 44
    • 0029095073 scopus 로고
    • Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase
    • A. Pandey, H. Duan, and V.M. Dixit Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase J. Biol. Chem. 270 1995 19201 19204
    • (1995) J. Biol. Chem. , vol.270 , pp. 19201-19204
    • Pandey, A.1    Duan, H.2    Dixit, V.M.3
  • 45
    • 0034602654 scopus 로고    scopus 로고
    • Analysis of receptor signaling pathways by mass spectrometry: Identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors
    • A. Pandey, A.V. Podtelejnikov, B. Blagoev, X.R. Bustelo, M. Mann, and H.F. Lodish Analysis of receptor signaling pathways by mass spectrometry: identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors Proc. Natl. Acad. Sci. USA 97 2000 179 184
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 179-184
    • Pandey, A.1    Podtelejnikov, A.V.2    Blagoev, B.3    Bustelo, X.R.4    Mann, M.5    Lodish, H.F.6
  • 47
    • 0032538792 scopus 로고    scopus 로고
    • Phosphorylation-dependent and constitutive activation of Rho proteins by wild-type and oncogenic Vav-2
    • K.E. Schuebel, N. Movilla, J.L. Rosa, and X.R. Bustelo Phosphorylation-dependent and constitutive activation of Rho proteins by wild-type and oncogenic Vav-2 EMBO J. 17 1998 6608 6621
    • (1998) EMBO J. , vol.17 , pp. 6608-6621
    • Schuebel, K.E.1    Movilla, N.2    Rosa, J.L.3    Bustelo, X.R.4
  • 48
    • 0141668894 scopus 로고    scopus 로고
    • Rac1 function is required for Src-induced transformation. Evidence of a role for Tiam1 and Vav2 in Rac activation by Src
    • J.M. Servitja, M.J. Marinissen, A. Sodhi, X.R. Bustelo, and J.S. Gutkind Rac1 function is required for Src-induced transformation. Evidence of a role for Tiam1 and Vav2 in Rac activation by Src J. Biol. Chem. 278 2003 34339 34346
    • (2003) J. Biol. Chem. , vol.278 , pp. 34339-34346
    • Servitja, J.M.1    Marinissen, M.J.2    Sodhi, A.3    Bustelo, X.R.4    Gutkind, J.S.5
  • 50
    • 0029813872 scopus 로고    scopus 로고
    • Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells
    • E. Stein, D.P. Cerretti, and T.O. Daniel Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells J. Biol. Chem. 271 1996 23588 23593
    • (1996) J. Biol. Chem. , vol.271 , pp. 23588-23593
    • Stein, E.1    Cerretti, D.P.2    Daniel, T.O.3
  • 51
    • 0031893255 scopus 로고    scopus 로고
    • Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase
    • E. Stein, U. Huynh-Do, A.A. Lane, D.P. Cerretti, and T.O. Daniel Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase J. Biol. Chem. 273 1998 1303 1308
    • (1998) J. Biol. Chem. , vol.273 , pp. 1303-1308
    • Stein, E.1    Huynh-Do, U.2    Lane, A.A.3    Cerretti, D.P.4    Daniel, T.O.5
  • 54
    • 0034977155 scopus 로고    scopus 로고
    • Membrane-targeting is critical for the phosphorylation of Vav2 by activated EGF receptor
    • P. Tamas, Z. Solti, and L. Buday Membrane-targeting is critical for the phosphorylation of Vav2 by activated EGF receptor Cell. Signal. 13 2001 475 481
    • (2001) Cell. Signal. , vol.13 , pp. 475-481
    • Tamas, P.1    Solti, Z.2    Buday, L.3
  • 56
    • 0029959555 scopus 로고    scopus 로고
    • The molecular biology of axon guidance
    • M. Tessier-Lavigne, and C.S. Goodman The molecular biology of axon guidance Science 274 1996 1123 1133
    • (1996) Science , vol.274 , pp. 1123-1133
    • Tessier-Lavigne, M.1    Goodman, C.S.2
  • 57
    • 1542723078 scopus 로고    scopus 로고
    • Unbiased analysis of bulk axonal segregation patterns
    • C.L. Torborg, and M.B. Feller Unbiased analysis of bulk axonal segregation patterns J. Neurosci. Methods 135 2004 17 26
    • (2004) J. Neurosci. Methods , vol.135 , pp. 17-26
    • Torborg, C.L.1    Feller, M.B.2
  • 58
    • 0036631548 scopus 로고    scopus 로고
    • VAV proteins as signal integrators for multi-subunit immune-recognition receptors
    • M. Turner, and D.D. Billadeau VAV proteins as signal integrators for multi-subunit immune-recognition receptors Nat. Rev. Immunol. 2 2002 476 486
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 476-486
    • Turner, M.1    Billadeau, D.D.2
  • 59
    • 0034678363 scopus 로고    scopus 로고
    • Ephrin-A5 induces collapse of growth cones by activating Rho and Rho kinase
    • S. Wahl, H. Barth, T. Ciossek, K. Aktories, and B.K. Mueller Ephrin-A5 induces collapse of growth cones by activating Rho and Rho kinase J. Cell Biol. 149 2000 263 270
    • (2000) J. Cell Biol. , vol.149 , pp. 263-270
    • Wahl, S.1    Barth, H.2    Ciossek, T.3    Aktories, K.4    Mueller, B.K.5
  • 60
    • 0033753734 scopus 로고    scopus 로고
    • The EphA4 receptor tyrosine kinase is necessary for the guidance of nasal retinal ganglion cell axons in vitro
    • J. Walkenhorst, D. Dutting, C. Handwerker, J. Huai, H. Tanaka, and U. Drescher The EphA4 receptor tyrosine kinase is necessary for the guidance of nasal retinal ganglion cell axons in vitro Mol. Cell. Neurosci. 16 2000 365 375
    • (2000) Mol. Cell. Neurosci. , vol.16 , pp. 365-375
    • Walkenhorst, J.1    Dutting, D.2    Handwerker, C.3    Huai, J.4    Tanaka, H.5    Drescher, U.6
  • 62
    • 0033776498 scopus 로고    scopus 로고
    • Role of phosphoinositide 3-kinase and endocytosis in nerve growth factor-induced extracellular signal-regulated kinase activation via Ras and Rap1
    • R.D. York, D.C. Molliver, S.S. Grewal, P.E. Stenberg, E.W. McCleskey, and P.J. Stork Role of phosphoinositide 3-kinase and endocytosis in nerve growth factor-induced extracellular signal-regulated kinase activation via Ras and Rap1 Mol. Cell. Biol. 20 2000 8069 8083
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8069-8083
    • York, R.D.1    Molliver, D.C.2    Grewal, S.S.3    Stenberg, P.E.4    McCleskey, E.W.5    Stork, P.J.6
  • 63
    • 0034255428 scopus 로고    scopus 로고
    • Cell surface Trk receptors mediate NGF-induced survival while internalized receptors regulate NGF-induced differentiation
    • Y. Zhang, D.B. Moheban, B.R. Conway, A. Bhattacharyya, and R.A. Segal Cell surface Trk receptors mediate NGF-induced survival while internalized receptors regulate NGF-induced differentiation J. Neurosci. 20 2000 5671 5678
    • (2000) J. Neurosci. , vol.20 , pp. 5671-5678
    • Zhang, Y.1    Moheban, D.B.2    Conway, B.R.3    Bhattacharyya, A.4    Segal, R.A.5
  • 64
    • 0141839883 scopus 로고    scopus 로고
    • EphB-ephrinB bi-directional endocytosis terminates adhesion allowing contact mediated repulsion
    • M. Zimmer, A. Palmer, J. Kohler, and R. Klein EphB-ephrinB bi-directional endocytosis terminates adhesion allowing contact mediated repulsion Nat. Cell Biol. 5 2003 869 878
    • (2003) Nat. Cell Biol. , vol.5 , pp. 869-878
    • Zimmer, M.1    Palmer, A.2    Kohler, J.3    Klein, R.4
  • 65
    • 0032554762 scopus 로고    scopus 로고
    • Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region
    • A.H. Zisch, M.S. Kalo, L.D. Chong, and E.B. Pasquale Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region Oncogene 16 1998 2657 2670
    • (1998) Oncogene , vol.16 , pp. 2657-2670
    • Zisch, A.H.1    Kalo, M.S.2    Chong, L.D.3    Pasquale, E.B.4
  • 66
    • 0034642564 scopus 로고    scopus 로고
    • Replacing two conserved tyrosines of the EphB2 receptor with glutamic acid prevents binding of SH2 domains without abrogating kinase activity and biological responses
    • A.H. Zisch, C. Pazzagli, A.L. Freeman, M. Schneller, M. Hadman, J.W. Smith, E. Ruoslahti, and E.B. Pasquale Replacing two conserved tyrosines of the EphB2 receptor with glutamic acid prevents binding of SH2 domains without abrogating kinase activity and biological responses Oncogene 19 2000 177 187
    • (2000) Oncogene , vol.19 , pp. 177-187
    • Zisch, A.H.1    Pazzagli, C.2    Freeman, A.L.3    Schneller, M.4    Hadman, M.5    Smith, J.W.6    Ruoslahti, E.7    Pasquale, E.B.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.