메뉴 건너뛰기




Volumn 18, Issue 5, 2006, Pages 533-540

Repulsion or adhesion: receptors make the call

Author keywords

[No Author keywords available]

Indexed keywords

EPHRIN; INTEGRIN; PLEXIN; SEMAPHORIN;

EID: 33748302057     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2006.08.010     Document Type: Review
Times cited : (48)

References (51)
  • 1
    • 0023544518 scopus 로고
    • Avoidance of posterior tectal membranes by temporal retinal axons
    • Walter J., Henke-Fahle S., and Bonhoeffer F. Avoidance of posterior tectal membranes by temporal retinal axons. Development 101 (1987) 909-913
    • (1987) Development , vol.101 , pp. 909-913
    • Walter, J.1    Henke-Fahle, S.2    Bonhoeffer, F.3
  • 2
    • 0024020967 scopus 로고
    • On the importance of being inhibited, or saying no to growth cones
    • Patterson P.H. On the importance of being inhibited, or saying no to growth cones. Neuron 1 (1988) 263-267
    • (1988) Neuron , vol.1 , pp. 263-267
    • Patterson, P.H.1
  • 3
    • 0022478279 scopus 로고
    • The selective inhibition of growth cone extension by specific neurites in culture
    • Kapfhammer J.P., Grunewald B.E., and Raper J.A. The selective inhibition of growth cone extension by specific neurites in culture. J Neurosci 6 (1986) 2527-2534
    • (1986) J Neurosci , vol.6 , pp. 2527-2534
    • Kapfhammer, J.P.1    Grunewald, B.E.2    Raper, J.A.3
  • 4
    • 0037817750 scopus 로고    scopus 로고
    • Signaling at the growth cone: ligand-receptor complexes and the control of axon growth and guidance
    • Huber A.B., Kolodkin A.L., Ginty D.D., and Cloutier J.F. Signaling at the growth cone: ligand-receptor complexes and the control of axon growth and guidance. Annu Rev Neurosci 26 (2003) 509-563
    • (2003) Annu Rev Neurosci , vol.26 , pp. 509-563
    • Huber, A.B.1    Kolodkin, A.L.2    Ginty, D.D.3    Cloutier, J.F.4
  • 5
    • 0034997358 scopus 로고    scopus 로고
    • Axon guidance at the midline choice point
    • Kaprielian Z., Runko E., and Imondi R. Axon guidance at the midline choice point. Dev Dyn 221 (2001) 154-181
    • (2001) Dev Dyn , vol.221 , pp. 154-181
    • Kaprielian, Z.1    Runko, E.2    Imondi, R.3
  • 6
    • 32344447055 scopus 로고    scopus 로고
    • Neural map specification by gradients
    • Flanagan J.G. Neural map specification by gradients. Curr Opin Neurobiol 16 (2006) 59-66
    • (2006) Curr Opin Neurobiol , vol.16 , pp. 59-66
    • Flanagan, J.G.1
  • 7
    • 20344396123 scopus 로고    scopus 로고
    • Eph receptor signalling casts a wide net on cell behaviour
    • Pasquale E.B. Eph receptor signalling casts a wide net on cell behaviour. Nat Rev Mol Cell Biol 6 (2005) 462-475
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 462-475
    • Pasquale, E.B.1
  • 8
    • 1842828975 scopus 로고    scopus 로고
    • Eph receptor-ephrin bidirectional signals that target Ras and Rho proteins
    • Noren N.K., and Pasquale E.B. Eph receptor-ephrin bidirectional signals that target Ras and Rho proteins. Cell Signal 16 (2004) 655-666
    • (2004) Cell Signal , vol.16 , pp. 655-666
    • Noren, N.K.1    Pasquale, E.B.2
  • 10
    • 25844431756 scopus 로고    scopus 로고
    • Touch and go: guidance cues signal to the growth cone cytoskeleton
    • Kalil K., and Dent E.W. Touch and go: guidance cues signal to the growth cone cytoskeleton. Curr Opin Neurobiol 15 (2005) 521-526
    • (2005) Curr Opin Neurobiol , vol.15 , pp. 521-526
    • Kalil, K.1    Dent, E.W.2
  • 11
    • 0346120154 scopus 로고    scopus 로고
    • Regulation of growth cone actin filaments by guidance cues
    • Gallo G., and Letourneau P.C. Regulation of growth cone actin filaments by guidance cues. J Neurobiol 58 (2004) 92-102
    • (2004) J Neurobiol , vol.58 , pp. 92-102
    • Gallo, G.1    Letourneau, P.C.2
  • 12
    • 0043182810 scopus 로고    scopus 로고
    • The function of semaphorins during nervous system development
    • Fiore R., and Puschel A.W. The function of semaphorins during nervous system development. Front Biosci 8 (2003) s484-s499
    • (2003) Front Biosci , vol.8
    • Fiore, R.1    Puschel, A.W.2
  • 13
    • 2442516485 scopus 로고    scopus 로고
    • To move or not to move? Semaphorin signalling in cell migration
    • Tamagnone L., and Comoglio P.M. To move or not to move? Semaphorin signalling in cell migration. EMBO Rep 5 (2004) 356-361
    • (2004) EMBO Rep , vol.5 , pp. 356-361
    • Tamagnone, L.1    Comoglio, P.M.2
  • 14
    • 20744434543 scopus 로고    scopus 로고
    • Plexins: axon guidance and signal transduction
    • Negishi M., Oinuma I., and Katoh H. Plexins: axon guidance and signal transduction. Cell Mol Life Sci 62 (2005) 1363-1371
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1363-1371
    • Negishi, M.1    Oinuma, I.2    Katoh, H.3
  • 16
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: biochemistry and biology
    • Jaffe A.B., and Hall A. Rho GTPases: biochemistry and biology. Annu Rev Cell Dev Biol 21 (2005) 247-269
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 17
    • 0033560132 scopus 로고    scopus 로고
    • Myelin and collapsin-1 induce motor neuron growth cone collapse through different pathways: inhibition of collapse by opposing mutants of rac1
    • Kuhn T.B., Brown M.D., Wilcox C.L., Raper J.A., and Bamburg J.R. Myelin and collapsin-1 induce motor neuron growth cone collapse through different pathways: inhibition of collapse by opposing mutants of rac1. J Neurosci 19 (1999) 1965-1975
    • (1999) J Neurosci , vol.19 , pp. 1965-1975
    • Kuhn, T.B.1    Brown, M.D.2    Wilcox, C.L.3    Raper, J.A.4    Bamburg, J.R.5
  • 18
    • 0034783680 scopus 로고    scopus 로고
    • Plexin B mediates axon guidance in Drosophila by simultaneously inhibiting active Rac and enhancing RhoA signaling
    • Hu H., Marton T.F., and Goodman C.S. Plexin B mediates axon guidance in Drosophila by simultaneously inhibiting active Rac and enhancing RhoA signaling. Neuron 32 (2001) 39-51
    • (2001) Neuron , vol.32 , pp. 39-51
    • Hu, H.1    Marton, T.F.2    Goodman, C.S.3
  • 19
    • 0030809301 scopus 로고    scopus 로고
    • Rac1 mediates collapsin-1-induced growth cone collapse
    • Jin Z., and Strittmatter S.M. Rac1 mediates collapsin-1-induced growth cone collapse. J Neurosci 17 (1997) 6256-6263
    • (1997) J Neurosci , vol.17 , pp. 6256-6263
    • Jin, Z.1    Strittmatter, S.M.2
  • 20
    • 0036206649 scopus 로고    scopus 로고
    • The plexin-B1/Rac interaction inhibits PAK activation and enhances Sema4D ligand binding
    • Vikis H.G., Li W., and Guan K.L. The plexin-B1/Rac interaction inhibits PAK activation and enhances Sema4D ligand binding. Genes Dev 16 (2002) 836-845
    • (2002) Genes Dev , vol.16 , pp. 836-845
    • Vikis, H.G.1    Li, W.2    Guan, K.L.3
  • 21
    • 0033598204 scopus 로고    scopus 로고
    • Sema3A-induced growth-cone collapse is mediated by Rac1 amino acids 17-32
    • Vastrik I., Eickholt B.J., Walsh F.S., Ridley A., and Doherty P. Sema3A-induced growth-cone collapse is mediated by Rac1 amino acids 17-32. Curr Biol 9 (1999) 991-998
    • (1999) Curr Biol , vol.9 , pp. 991-998
    • Vastrik, I.1    Eickholt, B.J.2    Walsh, F.S.3    Ridley, A.4    Doherty, P.5
  • 23
    • 4043105621 scopus 로고    scopus 로고
    • The activity of the plexin-A1 receptor is regulated by Rac
    • The authors were the first to demonstrate that Rac1 associates directly with PlexinA1 and that Rac1 is activated by Sema3A stimulation. Moreover, they show that constitutively active PlexinA1 does not require Rac1, suggesting that Rac1 acts upstream of PlexinA1 during Sema3A-induced repulsion.
    • Turner L.J., Nicholls S., and Hall A. The activity of the plexin-A1 receptor is regulated by Rac. J Biol Chem 279 (2004) 33199-33205. The authors were the first to demonstrate that Rac1 associates directly with PlexinA1 and that Rac1 is activated by Sema3A stimulation. Moreover, they show that constitutively active PlexinA1 does not require Rac1, suggesting that Rac1 acts upstream of PlexinA1 during Sema3A-induced repulsion.
    • (2004) J Biol Chem , vol.279 , pp. 33199-33205
    • Turner, L.J.1    Nicholls, S.2    Hall, A.3
  • 24
    • 28044451085 scopus 로고    scopus 로고
    • FARP2 triggers signals for Sema3A-mediated axonal repulsion
    • This study is crucial for bridging several gaps in our understanding of the signaling pathway linking Sema3A and integrin activity. The authors show that activation of Rac1 by Sema3A stimulation is dependent on FARP2's dissociation from PlexinA1. Furthermore, they showi that FARP2's RacGEF activity is critical for the association of Rnd1 with PlexinA1 and the stimulation of PlexinA1's R-Ras GAP activity.
    • Toyofuku T., Yoshida J., Sugimoto T., Zhang H., Kumanogoh A., Hori M., and Kikutani H. FARP2 triggers signals for Sema3A-mediated axonal repulsion. Nat Neurosci 8 (2005) 1712-1719. This study is crucial for bridging several gaps in our understanding of the signaling pathway linking Sema3A and integrin activity. The authors show that activation of Rac1 by Sema3A stimulation is dependent on FARP2's dissociation from PlexinA1. Furthermore, they showi that FARP2's RacGEF activity is critical for the association of Rnd1 with PlexinA1 and the stimulation of PlexinA1's R-Ras GAP activity.
    • (2005) Nat Neurosci , vol.8 , pp. 1712-1719
    • Toyofuku, T.1    Yoshida, J.2    Sugimoto, T.3    Zhang, H.4    Kumanogoh, A.5    Hori, M.6    Kikutani, H.7
  • 25
    • 0036813091 scopus 로고    scopus 로고
    • A novel FERM domain including guanine nucleotide exchange factor is involved in Rac signaling and regulates neurite remodeling
    • Kubo T., Yamashita T., Yamaguchi A., Sumimoto H., Hosokawa K., and Tohyama M. A novel FERM domain including guanine nucleotide exchange factor is involved in Rac signaling and regulates neurite remodeling. J Neurosci 22 (2002) 8504-8513
    • (2002) J Neurosci , vol.22 , pp. 8504-8513
    • Kubo, T.1    Yamashita, T.2    Yamaguchi, A.3    Sumimoto, H.4    Hosokawa, K.5    Tohyama, M.6
  • 26
    • 0037080330 scopus 로고    scopus 로고
    • Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse
    • Zanata S.M., Hovatta I., Rohm B., and Puschel A.W. Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse. J Neurosci 22 (2002) 471-477
    • (2002) J Neurosci , vol.22 , pp. 471-477
    • Zanata, S.M.1    Hovatta, I.2    Rohm, B.3    Puschel, A.W.4
  • 27
    • 3843065433 scopus 로고    scopus 로고
    • The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein for R-Ras
    • The authors were the first to show that the Sema4D receptor, PlexinB1, possesses intrinsic R-Ras GAP activity and to describe its regulation. They demonstrate that Rnd1-bound PlexinB1 directly downregulates R-Ras activity, which is necessary to achieve repulsion by Sema4D.
    • Oinuma I., Ishikawa Y., Katoh H., and Negishi M. The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein for R-Ras. Science 305 (2004) 862-865. The authors were the first to show that the Sema4D receptor, PlexinB1, possesses intrinsic R-Ras GAP activity and to describe its regulation. They demonstrate that Rnd1-bound PlexinB1 directly downregulates R-Ras activity, which is necessary to achieve repulsion by Sema4D.
    • (2004) Science , vol.305 , pp. 862-865
    • Oinuma, I.1    Ishikawa, Y.2    Katoh, H.3    Negishi, M.4
  • 29
    • 0033620657 scopus 로고    scopus 로고
    • R-Ras signals through specific integrin α cytoplasmic domains to promote migration and invasion of breast epithelial cells
    • Keely P.J., Rusyn E.V., Cox A.D., and Parise L.V. R-Ras signals through specific integrin α cytoplasmic domains to promote migration and invasion of breast epithelial cells. J Cell Biol 145 (1999) 1077-1088
    • (1999) J Cell Biol , vol.145 , pp. 1077-1088
    • Keely, P.J.1    Rusyn, E.V.2    Cox, A.D.3    Parise, L.V.4
  • 30
    • 0037038412 scopus 로고    scopus 로고
    • Type I γ phosphatidylinositol phosphate kinase targets and regulates focal adhesions
    • Ling K., Doughman R.L., Firestone A.J., Bunce M.W., and Anderson R.A. Type I γ phosphatidylinositol phosphate kinase targets and regulates focal adhesions. Nature 420 (2002) 89-93
    • (2002) Nature , vol.420 , pp. 89-93
    • Ling, K.1    Doughman, R.L.2    Firestone, A.J.3    Bunce, M.W.4    Anderson, R.A.5
  • 32
    • 0033739987 scopus 로고    scopus 로고
    • The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner
    • Vikis H.G., Li W., He Z., and Guan K.L. The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner. Proc Natl Acad Sci USA 97 (2000) 12457-12462
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12457-12462
    • Vikis, H.G.1    Li, W.2    He, Z.3    Guan, K.L.4
  • 33
    • 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
    • This paper demonstrates that Rnd1 relieves an intramolecular interaction between PlexinB1's two GAP domains, which is necessary to allow R-Ras-GTP to bind and be inactivated. Furthermore, the authors show that Sema4D-induced PlexinB1 clustering is also necessary to stimulate PlexinB1's R-Ras GAP activity.
    • Oinuma I., Katoh H., and 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 (2004) 11473-11480. This paper demonstrates that Rnd1 relieves an intramolecular interaction between PlexinB1's two GAP domains, which is necessary to allow R-Ras-GTP to bind and be inactivated. Furthermore, the authors show that Sema4D-induced PlexinB1 clustering is also necessary to stimulate PlexinB1's R-Ras GAP activity.
    • (2004) J Neurosci , vol.24 , pp. 11473-11480
    • Oinuma, I.1    Katoh, H.2    Negishi, M.3
  • 34
    • 0038491273 scopus 로고    scopus 로고
    • Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells
    • Oinuma I., Katoh H., Harada A., and Negishi M. Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells. J Biol Chem 278 (2003) 25671-25677
    • (2003) J Biol Chem , vol.278 , pp. 25671-25677
    • Oinuma, I.1    Katoh, H.2    Harada, A.3    Negishi, M.4
  • 35
    • 2442421626 scopus 로고    scopus 로고
    • Plexin signaling hampers integrin-based adhesion, leading to Rho-kinase independent cell rounding, and inhibiting lamellipodia extension and cell motility
    • Barberis D., Artigiani S., Casazza A., Corso S., Giordano S., Love C.A., Jones E.Y., Comoglio P.M., and Tamagnone L. Plexin signaling hampers integrin-based adhesion, leading to Rho-kinase independent cell rounding, and inhibiting lamellipodia extension and cell motility. FASEB J 18 (2004) 592-594
    • (2004) FASEB J , vol.18 , pp. 592-594
    • Barberis, D.1    Artigiani, S.2    Casazza, A.3    Corso, S.4    Giordano, S.5    Love, C.A.6    Jones, E.Y.7    Comoglio, P.M.8    Tamagnone, L.9
  • 36
    • 4744376056 scopus 로고    scopus 로고
    • Repulsion and attraction of axons by semaphorin3D are mediated by different neuropilins in vivo
    • Wolman M.A., Liu Y., Tawarayama H., Shoji W., and Halloran M.C. Repulsion and attraction of axons by semaphorin3D are mediated by different neuropilins in vivo. J Neurosci 24 (2004) 8428-8435
    • (2004) J Neurosci , vol.24 , pp. 8428-8435
    • Wolman, M.A.1    Liu, Y.2    Tawarayama, H.3    Shoji, W.4    Halloran, M.C.5
  • 37
    • 5044240692 scopus 로고    scopus 로고
    • Diverse roles of eph receptors and ephrins in the regulation of cell migration and tissue assembly
    • Poliakov A., Cotrina M., and Wilkinson D.G. Diverse roles of eph receptors and ephrins in the regulation of cell migration and tissue assembly. Dev Cell 7 (2004) 465-480
    • (2004) Dev Cell , vol.7 , pp. 465-480
    • Poliakov, A.1    Cotrina, M.2    Wilkinson, D.G.3
  • 38
    • 0036303033 scopus 로고    scopus 로고
    • Mechanisms and functions of Eph and ephrin signalling
    • Kullander K., and Klein R. 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
  • 39
    • 0031922119 scopus 로고    scopus 로고
    • The ephrins and Eph receptors in neural development
    • Flanagan J.G., and Vanderhaeghen P. 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
  • 40
    • 0141839882 scopus 로고    scopus 로고
    • Rac-dependent trans-endocytosis of ephrinBs regulates Eph-ephrin contact repulsion
    • Marston D.J., Dickinson S., and Nobes C.D. 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
  • 41
    • 0141839883 scopus 로고    scopus 로고
    • EphB-ephrinB bi-directional endocytosis terminates adhesion allowing contact-mediated repulsion
    • Zimmer M., Palmer A., Kohler J., and Klein R. 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
  • 42
    • 1642422313 scopus 로고    scopus 로고
    • Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2
    • Pascall J.C., and Brown K.D. Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2. Biochem Biophys Res Commun 317 (2004) 244-252
    • (2004) Biochem Biophys Res Commun , vol.317 , pp. 244-252
    • Pascall, J.C.1    Brown, K.D.2
  • 43
    • 0034714357 scopus 로고    scopus 로고
    • Regulated cleavage of a contact-mediated axon repellent
    • Hattori M., Osterfield M., and Flanagan J.G. 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
  • 44
    • 26844448800 scopus 로고    scopus 로고
    • Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans
    • The authors show that the ADAM10 metalloprotease is associated in cis with EphA and cleaves ephrinA in trans. They also show that the ADAM10 cysteine-rich domain specifically recognizes an ephrinA-EphA complex and only then activates the protease domain. This provides a mechanism by which ADAM10 selectively cleaves only Eph-bound ephrins.
    • Janes P.W., Saha N., Barton W.A., Kolev M.V., Wimmer-Kleikamp S.H., Nievergall E., Blobel C.P., Himanen J.P., Lackmann M., and Nikolov D.B. Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans. Cell 123 (2005) 291-304. The authors show that the ADAM10 metalloprotease is associated in cis with EphA and cleaves ephrinA in trans. They also show that the ADAM10 cysteine-rich domain specifically recognizes an ephrinA-EphA complex and only then activates the protease domain. This provides a mechanism by which ADAM10 selectively cleaves only Eph-bound ephrins.
    • (2005) Cell , vol.123 , pp. 291-304
    • Janes, P.W.1    Saha, N.2    Barton, W.A.3    Kolev, M.V.4    Wimmer-Kleikamp, S.H.5    Nievergall, E.6    Blobel, C.P.7    Himanen, J.P.8    Lackmann, M.9    Nikolov, D.B.10
  • 45
    • 0034626791 scopus 로고    scopus 로고
    • Regulation of repulsion versus adhesion by different splice forms of an Eph receptor
    • Holmberg J., Clarke D.L., and Frisen J. Regulation of repulsion versus adhesion by different splice forms of an Eph receptor. Nature 408 (2000) 203-206
    • (2000) Nature , vol.408 , pp. 203-206
    • Holmberg, J.1    Clarke, D.L.2    Frisen, J.3
  • 47
    • 1242316215 scopus 로고    scopus 로고
    • EphA receptor tyrosine kinases interact with co-expressed ephrin-A ligands in cis
    • Yin Y., Yamashita Y., Noda H., Okafuji T., Go M.J., and Tanaka H. EphA receptor tyrosine kinases interact with co-expressed ephrin-A ligands in cis. Neurosci Res 48 (2004) 285-296
    • (2004) Neurosci Res , vol.48 , pp. 285-296
    • Yin, Y.1    Yamashita, Y.2    Noda, H.3    Okafuji, T.4    Go, M.J.5    Tanaka, H.6
  • 49
    • 33344477193 scopus 로고    scopus 로고
    • Silencing of EphA3 through a cis interaction with ephrinA5
    • This study reveals a mechanism by which cis-expressed ephrinA5 can block EphA3 phosphorylation through an interaction with the fibronectin III domain of EphA3. This silences EphA3 signaling and reduces the response of the cell to ephrinA presented in trans.
    • Carvalho R.F., Beutler M., Marler K.J., Knoll B., Becker-Barroso E., Heintzmann R., Ng T., and Drescher U. Silencing of EphA3 through a cis interaction with ephrinA5. Nat Neurosci 9 (2006) 322-330. This study reveals a mechanism by which cis-expressed ephrinA5 can block EphA3 phosphorylation through an interaction with the fibronectin III domain of EphA3. This silences EphA3 signaling and reduces the response of the cell to ephrinA presented in trans.
    • (2006) Nat Neurosci , vol.9 , pp. 322-330
    • Carvalho, R.F.1    Beutler, M.2    Marler, K.J.3    Knoll, B.4    Becker-Barroso, E.5    Heintzmann, R.6    Ng, T.7    Drescher, U.8
  • 50
    • 2942534978 scopus 로고    scopus 로고
    • Retinal axon response to ephrin-as shows a graded, concentration-dependent transition from growth promotion to inhibition
    • The authors demonstrate that retinal axons respond with either attraction or repulsion to ephrinA5, depending on their retinal region of origin and on the concentration of ephrinA5 they encounter. They propose a model to explain how retinal axons target to the correct location on the tectal ephrinA5 gradient by regulating the balance between ephrin-Eph-mediated adhesion versus repulsion.
    • Hansen M.J., Dallal G.E., and Flanagan J.G. Retinal axon response to ephrin-as shows a graded, concentration-dependent transition from growth promotion to inhibition. Neuron 42 (2004) 717-730. The authors demonstrate that retinal axons respond with either attraction or repulsion to ephrinA5, depending on their retinal region of origin and on the concentration of ephrinA5 they encounter. They propose a model to explain how retinal axons target to the correct location on the tectal ephrinA5 gradient by regulating the balance between ephrin-Eph-mediated adhesion versus repulsion.
    • (2004) Neuron , vol.42 , pp. 717-730
    • Hansen, M.J.1    Dallal, G.E.2    Flanagan, J.G.3
  • 51
    • 17044377138 scopus 로고    scopus 로고
    • Coexpressed EphA receptors and ephrin-A ligands mediate opposing actions on growth cone navigation from distinct membrane domains
    • The authors show that in motor axons, cis EphA and ephrinA are separated into distinct membrane domains that restrict their cis interactions. This mechanism allows independent signaling from ephrins and Ephs expressed in the same cell membrane.
    • Marquardt T., Shirasaki R., Ghosh S., Andrews S.E., Carter N., Hunter T., and Pfaff S.L. Coexpressed EphA receptors and ephrin-A ligands mediate opposing actions on growth cone navigation from distinct membrane domains. Cell 121 (2005) 127-139. The authors show that in motor axons, cis EphA and ephrinA are separated into distinct membrane domains that restrict their cis interactions. This mechanism allows independent signaling from ephrins and Ephs expressed in the same cell membrane.
    • (2005) Cell , vol.121 , pp. 127-139
    • Marquardt, T.1    Shirasaki, R.2    Ghosh, S.3    Andrews, S.E.4    Carter, N.5    Hunter, T.6    Pfaff, S.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.