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Volumn 216, Issue 1, 2017, Pages 199-215

A reverse signaling pathway downstream of Sema4A controls cell migration via Scrib

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; PLEXIN; PLEXIN B1; PROTEIN; PROTEIN CDC42; PROTEIN SCRIB; RAC PROTEIN; RAC1 PROTEIN; SEMAPHORIN; SEMAPHORIN 4A; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; CELL SURFACE RECEPTOR; MEMBRANE PROTEIN; NERVE PROTEIN; PLXNB1 PROTEIN, HUMAN; PLXNB1 PROTEIN, MOUSE; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR; SCRIB PROTEIN, HUMAN; SCRIBBLE PROTEIN, MOUSE; SEMA4A PROTEIN, HUMAN; SEMA4A PROTEIN, MOUSE; SIGNAL PEPTIDE; TUMOR SUPPRESSOR PROTEIN;

EID: 85008674821     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201602002     Document Type: Article
Times cited : (30)

References (90)
  • 1
    • 84923072347 scopus 로고    scopus 로고
    • Circulating semaphorin-4D and plexin-B1 levels in postmenopausal women with low bone mass: The 3-month effect of zoledronic acid, denosumab or teriparatide treatment
    • Anastasilakis, A.D., S.A. Polyzos, P. Makras, A. Gkiomisi, G. Sakellariou, M. Savvidis, A. Papatheodorou, P. Kokkoris, and E. Terpos. 2015. Circulating semaphorin-4D and plexin-B1 levels in postmenopausal women with low bone mass: the 3-month effect of zoledronic acid, denosumab or teriparatide treatment. Expert Opin. Ther. Targets. 19:299-306. http://dx.doi.org/10.1517/14728222.2014.983078
    • (2015) Expert Opin. Ther. Targets , vol.19 , pp. 299-306
    • Anastasilakis, A.D.1    Polyzos, S.A.2    Makras, P.3    Gkiomisi, A.4    Sakellariou, G.5    Savvidis, M.6    Papatheodorou, A.7    Kokkoris, P.8    Terpos, E.9
  • 3
    • 84155167012 scopus 로고    scopus 로고
    • Expression of Semaphorin 4F in neurons and brain oligodendrocytes and the regulation of oligodendrocyte precursor migration in the optic nerve
    • Artigiani, S., D. Barberis, P. Fazzari, P. Longati, P. Angelini, J.W. vande
    • Armendáriz, B.G., A. Bribian, E. Pérez-Martínez, A. Martínez, F. de Castro, E. Soriano, and F. Burgaya. 2012. Expression of Semaphorin 4F in neurons and brain oligodendrocytes and the regulation of oligodendrocyte precursor migration in the optic nerve. Mol. Cell. Neurosci. 49:54-67. http://dx.doi.org/10.1016/j.mcn.2011.09.003Artigiani, S., D.Barberis, P.Fazzari, P.Longati, P.Angelini, J.W.vande
    • (2012) Mol. Cell. Neurosci , vol.49 , pp. 54-67
    • Armendáriz, B.G.1    Bribian, A.2    Pérez-Martínez, E.3    Martínez, A.4    de Castro, F.5    Soriano, E.6    Burgaya, F.7
  • 4
    • 0038532245 scopus 로고    scopus 로고
    • Functional regulation of semaphorin receptors by proprotein convertases
    • Loo, P.M. Comoglio, and L. Tamagnone. 2003. Functional regulation of semaphorin receptors by proprotein convertases. J. Biol. Chem. 278:10094-10101. http://dx.doi.org/10.1074/jbc.M210156200
    • (2003) J. Biol. Chem , vol.278 , pp. 10094-10101
    • Loo, P.M.C.1    Tamagnone, L.2
  • 6
    • 23344446919 scopus 로고    scopus 로고
    • Semaphorin 4D/plexin-B1 induces endothelial cell migration through the activation of PYK2, Src, and the phosphatidylinositol 3-kinase-Akt pathway
    • Basile, J.R., T. Afkhami, and J.S. Gutkind. 2005. Semaphorin 4D/plexin-B1 induces endothelial cell migration through the activation of PYK2, Src, and the phosphatidylinositol 3-kinase-Akt pathway. Mol. Cell. Biol. 25:6889-6898. http://dx.doi.org/10.1128/MCB.25.16.6889-6898.2005
    • (2005) Mol. Cell. Biol , vol.25 , pp. 6889-6898
    • Basile, J.R.1    Afkhami, T.2    Gutkind, J.S.3
  • 7
    • 84955292584 scopus 로고    scopus 로고
    • Transmembrane semaphorins, forward and reverse signaling: Have a look both ways
    • Battistini, C., and L. Tamagnone. 2016. Transmembrane semaphorins, forward and reverse signaling: have a look both ways. L. Cell. Mol. Life Sci. 73:1609-1622.
    • (2016) L. Cell. Mol. Life Sci , vol.73 , pp. 1609-1622
    • Battistini, C.1    Tamagnone, L.2
  • 9
    • 21244431997 scopus 로고    scopus 로고
    • Semaphorin 4B interacts with the post-synaptic density protein PSD-95/SAP90 and is recruited to synapses through a C-terminal PDZ-binding motif
    • Burkhardt, C., M. Müller, A. Badde, C.C. Garner, E.D. Gundelfinger, and A.W. Püschel. 2005. Semaphorin 4B interacts with the post-synaptic density protein PSD-95/SAP90 and is recruited to synapses through a C-terminal PDZ-binding motif. FEBS Lett. 579:3821-3828. http://dx.doi.org/10.1016/j.febslet.2005.05.079
    • (2005) FEBS Lett , vol.579 , pp. 3821-3828
    • Burkhardt, C.1    Müller, M.2    Badde, A.3    Garner, C.C.4    Gundelfinger, E.D.5    Püschel, A.W.6
  • 10
    • 33646085338 scopus 로고    scopus 로고
    • Semaphorin-1a functions as a guidance receptor in the Drosophila visual system
    • Cafferty, P., L. Yu, H. Long, and Y. Rao. 2006. Semaphorin-1a functions as a guidance receptor in the Drosophila visual system. J. Neurosci. 26:3999-4003. http://dx.doi.org/10.1523/JNEUROSCI.3845-05.2006
    • (2006) J. Neurosci , vol.26 , pp. 3999-4003
    • Cafferty, P.1    Yu, L.2    Long, H.3    Rao, Y.4
  • 11
    • 84934444702 scopus 로고    scopus 로고
    • Semaphorin signals in cell adhesion and cell migration: Functional role and molecular mechanisms
    • Casazza, A., P. Fazzari, and L. Tamagnone. 2007. Semaphorin signals in cell adhesion and cell migration: functional role and molecular mechanisms. Adv. Exp. Med. Biol. 600:90-108. http://dx.doi.org/10.1007/978-0-387-70956-78
    • (2007) Adv. Exp. Med. Biol , vol.600 , pp. 90-108
    • Casazza, A.1    Fazzari, P.2    Tamagnone, L.3
  • 12
    • 80055047330 scopus 로고    scopus 로고
    • Control of bone resorption by semaphorin 4D is dependent on ovarian function
    • Dacquin, R., C. Domenget, A. Kumanogoh, H. Kikutani, P. Jurdic, and I. Machuca-Gayet. 2011. Control of bone resorption by semaphorin 4D is dependent on ovarian function. PLoS One. 6. http://dx.doi.org/10.1371/journal.pone.0026627
    • (2011) PLoS One , pp. 6
    • Dacquin, R.1    Domenget, C.2    Kumanogoh, A.3    Kikutani, H.4    Jurdic, P.5    McHuca-Gayet, I.6
  • 14
    • 34147094240 scopus 로고    scopus 로고
    • The tumour-suppressor Scribble dictates cell polarity during directed epithelial migration: Regulation of Rho GTPase recruitment to the leading edge
    • Dow, L.E., J.S. Kauffman, J. Caddy, K. Zarbalis, A.S. Peterson, S.M. Jane, S.M. Russell, and P.O. Humbert. 2007. The tumour-suppressor Scribble dictates cell polarity during directed epithelial migration: regulation of Rho GTPase recruitment to the leading edge. Oncogene. 26:2272-2282. http://dx.doi.org/10.1038/sj.onc.1210016
    • (2007) Oncogene , vol.26 , pp. 2272-2282
    • Dow, L.E.1    Kauffman, J.S.2    Caddy, J.3    Zarbalis, K.4    Peterson, A.S.5    Jane, S.M.6    Russell, S.M.7    Humbert, P.O.8
  • 15
    • 53649108148 scopus 로고    scopus 로고
    • Loss of human Scribble cooperates with H-Ras to promote cell invasion through deregulation of MAPK signalling
    • Dow, L.E., I.A. Elsum, C.L. King, K.M. Kinross, H.E. Richardson, and P.O. Humbert. 2008. Loss of human Scribble cooperates with H-Ras to promote cell invasion through deregulation of MAPK signalling. Oncogene. 27:5988-6001. http://dx.doi.org/10.1038/onc.2008.219
    • (2008) Oncogene , vol.27 , pp. 5988-6001
    • Dow, L.E.1    Elsum, I.A.2    King, C.L.3    Kinross, K.M.4    Richardson, H.E.5    Humbert, P.O.6
  • 16
    • 0035814887 scopus 로고    scopus 로고
    • Plexin-B semaphorin receptors interact directly with active Rac and regulate the actin cytoskeleton by activating Rho
    • Driessens, M.H., H. Hu, C.D. Nobes, A. Self, I. Jordens, C.S. Goodman, and A. Hall. 2001. Plexin-B semaphorin receptors interact directly with active Rac and regulate the actin cytoskeleton by activating Rho. Curr. Biol. 11:339-344. http://dx.doi.org/10.1016/S0960-9822(01)00092-6
    • (2001) Curr. Biol , vol.11 , pp. 339-344
    • Driessens, M.H.1    Hu, H.2    Nobes, C.D.3    Self, A.4    Jordens, I.5    Goodman, C.S.6    Hall, A.7
  • 18
    • 84871909004 scopus 로고    scopus 로고
    • The Scribble-Dlg-Lgl polarity module in development and cancer: From flies to man
    • Elsum, I., L. Yates, P.O. Humbert, and H.E. Richardson. 2012. The Scribble-Dlg-Lgl polarity module in development and cancer: from flies to man. Essays Biochem. 53:141-168. http://dx.doi.org/10.1042/bse0530141
    • (2012) Essays Biochem , vol.53 , pp. 141-168
    • Elsum, I.1    Yates, L.2    Humbert, P.O.3    Richardson, H.E.4
  • 21
    • 84945244485 scopus 로고    scopus 로고
    • SrGAP2-dependent integration of membrane geometry and Slit-Robo-repulsive cues regulates fibroblast contact inhibition of locomotion
    • Fritz, R.D., D. Menshykau, K. Martin, A. Reimann, V. Pontelli, and O. Pertz. 2015. SrGAP2-dependent integration of membrane geometry and Slit-Robo-repulsive cues regulates fibroblast contact inhibition of locomotion. Dev. Cell. 35:78-92. http://dx.doi.org/10.1016/j.devcel.2015.09.002
    • (2015) Dev. Cell , vol.35 , pp. 78-92
    • Fritz, R.D.1    Menshykau, D.2    Martin, K.3    Reimann, A.4    Pontelli, V.5    Pertz, O.6
  • 22
    • 70350532478 scopus 로고    scopus 로고
    • A model of anti-angiogenesis: Differential transcriptosome profiling of microvascular endothelial cells from diffuse systemic sclerosis patients
    • Giusti, B., G. Fibbi, F. Margheri, S. Serratì, L. Rossi, F. Poggi, I. Lapini, A. Magi, A. Del Rosso, M. Cinelli, et al. 2006. A model of anti-angiogenesis: differential transcriptosome profiling of microvascular endothelial cells from diffuse systemic sclerosis patients. Arthritis Res. Ther. 8. http://dx.doi.org/10.1186/ar2002
    • (2006) Arthritis Res. Ther , pp. 8
    • Giusti, B.1    Fibbi, G.2    Margheri, F.3    Serratì, S.4    Rossi, L.5    Poggi, F.6    Lapini, I.7    Magi, A.8    Del Rosso, A.9    Cinelli, M.10
  • 23
    • 80053111149 scopus 로고    scopus 로고
    • Regulating Rap small G-proteins in time and space
    • Gloerich, M., and J.L. Bos. 2011. Regulating Rap small G-proteins in time and space. Trends Cell Biol. 21:615-623. http://dx.doi.org/10.1016/j.tcb.2011.07.001
    • (2011) Trends Cell Biol , vol.21 , pp. 615-623
    • Gloerich, M.1    Bos, J.L.2
  • 24
    • 0036897580 scopus 로고    scopus 로고
    • Bi-directional signaling by Semaphorin 1a during central synapse formation in Drosophila
    • Godenschwege, T.A., H. Hu, X. Shan-Crofts, C.S. Goodman, and R.K. Murphey. 2002. Bi-directional signaling by Semaphorin 1a during central synapse formation in Drosophila. Nat. Neurosci. 5:1294-1301. http://dx.doi.org/10.1038/nn976
    • (2002) Nat. Neurosci , vol.5 , pp. 1294-1301
    • Godenschwege, T.A.1    Hu, H.2    Shan-Crofts, X.3    Goodman, C.S.4    Murphey, R.K.5
  • 25
    • 84921742903 scopus 로고    scopus 로고
    • I'm coming to GEF you: Regulation of RhoGEFs during cell migration
    • Goicoechea, S.M., S. Awadia, and R. Garcia-Mata. 2014. I'm coming to GEF you: Regulation of RhoGEFs during cell migration. Cell Adhes. Migr. 8:535-549. http://dx.doi.org/10.4161/cam.28721
    • (2014) Cell Adhes. Migr , vol.8 , pp. 535-549
    • Goicoechea, S.M.1    Awadia, S.2    Garcia-Mata, R.3
  • 27
    • 84877138671 scopus 로고    scopus 로고
    • The role of semaphorins and their receptors in vascular development and cancer
    • Gu, C., and E. Giraudo. 2013. The role of semaphorins and their receptors in vascular development and cancer. Exp. Cell Res. 319:1306-1316. http://dx.doi.org/10.1016/j.yexcr.2013.02.003
    • (2013) Exp. Cell Res , vol.319 , pp. 1306-1316
    • Gu, C.1    Giraudo, E.2
  • 28
    • 84978141450 scopus 로고    scopus 로고
    • Transmembrane semaphorins: Multimodal signaling cues in development and cancer
    • Gurrapu, S., and L. Tamagnone. 2016. Transmembrane semaphorins: multimodal signaling cues in development and cancer. Cell Adhes. Migr. 10:675-691. http://dx.doi.org/10.1007/978-0-387-70956-78
    • (2016) Cell Adhes. Migr , vol.10 , pp. 675-691
    • Gurrapu, S.1    Tamagnone, L.2
  • 29
    • 84900425523 scopus 로고    scopus 로고
    • A new genetically encoded single-chain biosensor for Cdc42 based on FRET, useful for live-cell imaging
    • Hanna, S., V. Miskolci, D. Cox, and L. Hodgson. 2014. A new genetically encoded single-chain biosensor for Cdc42 based on FRET, useful for live-cell imaging. PLoS One. 9. http://dx.doi.org/10.1371/journal.pone.0096469
    • (2014) PLoS One , pp. 9
    • Hanna, S.1    Miskolci, V.2    Cox, D.3    Hodgson, L.4
  • 30
    • 77954051527 scopus 로고    scopus 로고
    • Identification of β-secretase (BACE1) substrates using quantitative proteomics
    • Hemming, M.L., J.E. Elias, S.P. Gygi, and D.J. Selkoe. 2009. Identification of β-secretase (BACE1) substrates using quantitative proteomics. PLoS One. 4. http://dx.doi.org/10.1371/journal.pone.0008477
    • (2009) PLoS One , pp. 4
    • Hemming, M.L.1    Elias, J.E.2    Gygi, S.P.3    Selkoe, D.J.4
  • 32
    • 84867848485 scopus 로고    scopus 로고
    • Plexin structures are coming: Opportunities for multilevel investigations of semaphorin guidance receptors, their cell signaling mechanisms, and functions
    • Hota, P.K., and M. Buck. 2012. Plexin structures are coming: opportunities for multilevel investigations of semaphorin guidance receptors, their cell signaling mechanisms, and functions. Cell. Mol. Life Sci. 69:3765-3805. http://dx.doi.org/10.1007/s00018-012-1019-0
    • (2012) Cell. Mol. Life Sci , vol.69 , pp. 3765-3805
    • Hota, P.K.1    Buck, M.2
  • 33
    • 0026481133 scopus 로고
    • Generation of large numbers of dendritic cells from mouse bone marrow cultures supplemented with granulocyte/ macrophage colony-stimulating factor
    • Inaba, K., M. Inaba, N. Romani, H. Aya, M. Deguchi, S. Ikehara, S. Muramatsu, and R.M. Steinman. 1992. Generation of large numbers of dendritic cells from mouse bone marrow cultures supplemented with granulocyte/ macrophage colony-stimulating factor. J. Exp. Med. 176:1693-1702. http://dx.doi.org/10.1084/jem.176.6.1693
    • (1992) J. Exp. Med , vol.176 , pp. 1693-1702
    • Inaba, K.1    Inaba, M.2    Romani, N.3    Aya, H.4    Deguchi, M.5    Ikehara, S.6    Muramatsu, S.7    Steinman, R.M.8
  • 35
    • 84901330536 scopus 로고    scopus 로고
    • Estrogen-dependent proteolytic cleavage of semaphorin 4D and plexin-B1 enhances semaphorin 4D-induced apoptosis during postnatal vaginal remodeling in pubescent mice
    • Ito, T., T. Bai, T. Tanaka, K. Yoshida, T. Ueyama, M. Miyajima, T. Negishi, T. Kawasaki, H. Takamatsu, H. Kikutani, et al. 2014. Estrogen-dependent proteolytic cleavage of semaphorin 4D and plexin-B1 enhances semaphorin 4D-induced apoptosis during postnatal vaginal remodeling in pubescent mice. PLoS One. 9. http://dx.doi.org/10.1371/journal.pone.0097909
    • (2014) PLoS One , pp. 9
    • Ito, T.1    Bai, T.2    Tanaka, T.3    Yoshida, K.4    Ueyama, T.5    Miyajima, M.6    Negishi, T.7    Kawasaki, T.8    Takamatsu, H.9    Kikutani, H.10
  • 37
    • 84906243388 scopus 로고    scopus 로고
    • Semaphorin signalling during development
    • Jongbloets, B.C., and R.J. Pasterkamp. 2014. Semaphorin signalling during development. Development. 141:3292-3297. http://dx.doi.org/10.1242/dev.105544
    • (2014) Development , vol.141 , pp. 3292-3297
    • Jongbloets, B.C.1    Pasterkamp, R.J.2
  • 38
    • 84875630392 scopus 로고    scopus 로고
    • Semaphorins in bone development, homeostasis, and disease
    • Kang, S., and A. Kumanogoh. 2013. Semaphorins in bone development, homeostasis, and disease. Semin. Cell Dev. Biol. 24:163-171. http://dx.doi.org/10.1016/j.semcdb.2012.09.008
    • (2013) Semin. Cell Dev. Biol , vol.24 , pp. 163-171
    • Kang, S.1    Kumanogoh, A.2
  • 39
    • 79951981589 scopus 로고    scopus 로고
    • Spatiotemporal regulation of small GTPases as revealed by probes based on the principle of Förster resonance energy transfer (FRET): Implications for signaling and pharmacology
    • Kiyokawa, E., K. Aoki, T. Nakamura, and M. Matsuda. 2011. Spatiotemporal regulation of small GTPases as revealed by probes based on the principle of Förster resonance energy transfer (FRET): Implications for signaling and pharmacology. Annu. Rev. Pharmacol. Toxicol. 51:337-358. http://dx.doi.org/10.1146/annurev-pharmtox-010510-100234
    • (2011) Annu. Rev. Pharmacol. Toxicol , vol.51 , pp. 337-358
    • Kiyokawa, E.1    Aoki, K.2    Nakamura, T.3    Matsuda, M.4
  • 40
    • 0027787683 scopus 로고
    • The semaphorin genes encode a family of transmembrane and secreted growth cone guidance molecules
    • Kolodkin, A.L., D.J. Matthes, and C.S. Goodman. 1993. The semaphorin genes encode a family of transmembrane and secreted growth cone guidance molecules. Cell. 75:1389-1399. http://dx.doi.org/10.1016/0092-8674(93)90625-Z
    • (1993) Cell , vol.75 , pp. 1389-1399
    • Kolodkin, A.L.1    Matthes, D.J.2    Goodman, C.S.3
  • 41
    • 33846302855 scopus 로고    scopus 로고
    • Graded expression of semaphorin-1a cell-autonomously directs dendritic targeting of olfactory projection neurons
    • Komiyama, T., L.B. Sweeney, O. Schuldiner, K.C. Garcia, and L. Luo. 2007. Graded expression of semaphorin-1a cell-autonomously directs dendritic targeting of olfactory projection neurons. Cell. 128:399-410. http://dx.doi.org/10.1016/j.cell.2006.12.028
    • (2007) Cell , vol.128 , pp. 399-410
    • Komiyama, T.1    Sweeney, L.B.2    Schuldiner, O.3    Garcia, K.C.4    Luo, L.5
  • 42
  • 45
    • 84902455455 scopus 로고    scopus 로고
    • The on-off relationship of Rho and Rac during integrin-mediated adhesion and cell migration
    • Lawson, C.D., and K. Burridge. 2014. The on-off relationship of Rho and Rac during integrin-mediated adhesion and cell migration. Small GTPases. 5. http://dx.doi.org/10.4161/sgtp.27958
    • (2014) Small GTPases , pp. 5
    • Lawson, C.D.1    Burridge, K.2
  • 46
    • 0141507038 scopus 로고    scopus 로고
    • The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D
    • Love, C.A., K. Harlos, N. Mavaddat, S.J. Davis, D.I. Stuart, E.Y. Jones, and R.M. Esnouf. 2003. The ligand-binding face of the semaphorins revealed by the high-resolution crystal structure of SEMA4D. Nat. Struct. Biol. 10:843-848. http://dx.doi.org/10.1038/nsb977
    • (2003) Nat. Struct. Biol , vol.10 , pp. 843-848
    • Love, C.A.1    Harlos, K.2    Mavaddat, N.3    Davis, S.J.4    Stuart, D.I.5    Jones, E.Y.6    Esnouf, R.M.7
  • 47
    • 0027373701 scopus 로고
    • Collapsin: A protein in brain that induces the collapse and paralysis of neuronal growth cones
    • Luo, Y., D. Raible, and J.A. Raper. 1993. Collapsin: a protein in brain that induces the collapse and paralysis of neuronal growth cones. Cell. 75:217-227. http://dx.doi.org/10.1016/0092-8674(93)80064-L
    • (1993) Cell , vol.75 , pp. 217-227
    • Luo, Y.1    Raible, D.2    Raper, J.A.3
  • 49
    • 84959353747 scopus 로고    scopus 로고
    • Spatio-temporal co-ordination of RhoA, Rac1 and Cdc42 activation during prototypical edge protrusion and retraction dynamics
    • Martin, K., A. Reimann, R.D. Fritz, H. Ryu, N.L. Jeon, and O. Pertz. 2016. Spatio-temporal co-ordination of RhoA, Rac1 and Cdc42 activation during prototypical edge protrusion and retraction dynamics. Sci. Rep. 6. http://dx.doi.org/10.1038/srep21901
    • (2016) Sci. Rep , pp. 6
    • Martin, K.1    Reimann, A.2    Fritz, R.D.3    Ryu, H.4    Jeon, N.L.5    Pertz, O.6
  • 50
    • 84885980407 scopus 로고    scopus 로고
    • Semaphorin signaling in the development and function of the gonadotropin hormone-releasing hormone system
    • Messina, A., and P. Giacobini. 2013. Semaphorin signaling in the development and function of the gonadotropin hormone-releasing hormone system. Front. Endocrinol. (Lausanne). 4.
    • (2013) Front. Endocrinol. (Lausanne) , pp. 4
    • Messina, A.1    Giacobini, P.2
  • 51
    • 84878661687 scopus 로고    scopus 로고
    • CD74-dependent deregulation of the tumor suppressor scribble in human epithelial and breast cancer cells
    • Metodieva, G., N.C. Nogueira-de-Souza, C. Greenwood, K. Al-Janabi, L. Leng, R. Bucala, and M.V. Metodiev. 2013. CD74-dependent deregulation of the tumor suppressor scribble in human epithelial and breast cancer cells. Neoplasia. 15:660-668. http://dx.doi.org/10.1593/neo.13464
    • (2013) Neoplasia , vol.15 , pp. 660-668
    • Metodieva, G.1    Nogueira-de-Souza, N.C.2    Greenwood, C.3    Al-Janabi, K.4    Leng, L.5    Bucala, R.6    Metodiev, M.V.7
  • 53
    • 66949135462 scopus 로고    scopus 로고
    • βPIX-activated Rac1 stimulates the activation of phospholipase D, which is associated with exocytosis in neuroendocrine cells
    • Momboisse, F., E. Lonchamp, V. Calco, M. Ceridono, N. Vitale, M.F. Bader, and S. Gasman. 2009. βPIX-activated Rac1 stimulates the activation of phospholipase D, which is associated with exocytosis in neuroendocrine cells. J. Cell Sci. 122:798-806. http://dx.doi.org/10.1242/jcs.038109
    • (2009) J. Cell Sci , vol.122 , pp. 798-806
    • Momboisse, F.1    Lonchamp, E.2    Calco, V.3    Ceridono, M.4    Vitale, N.5    Bader, M.F.6    Gasman, S.7
  • 55
    • 84861110359 scopus 로고    scopus 로고
    • Elevation of Sema4A implicates Th cell skewing and the efficacy of IFN-β therapy in multiple sclerosis
    • Nakatsuji, Y., T. Okuno, M. Moriya, T. Sugimoto, M. Kinoshita, H. Takamatsu, S. Nojima, T. Kimura, S. Kang, D. Ito, et al. 2012. Elevation of Sema4A implicates Th cell skewing and the efficacy of IFN-β therapy in multiple sclerosis. J. Immunol. 188:4858-4865. http://dx.doi.org/10.4049/jimmunol.1102023
    • (2012) J. Immunol , vol.188 , pp. 4858-4865
    • Nakatsuji, Y.1    Okuno, T.2    Moriya, M.3    Sugimoto, T.4    Kinoshita, M.5    Takamatsu, H.6    Nojima, S.7    Kimura, T.8    Kang, S.9    Ito, D.10
  • 57
    • 37149014854 scopus 로고    scopus 로고
    • Differential gene expression of primary cultured lymphatic and blood vascular endothelial cells
    • Nelson, G.M., T.P. Padera, I. Garkavtsev, T. Shioda, and R.K. Jain. 2007. Differential gene expression of primary cultured lymphatic and blood vascular endothelial cells. Neoplasia. 9:1038-1045. http://dx.doi.org/10.1593/neo.07643
    • (2007) Neoplasia , vol.9 , pp. 1038-1045
    • Nelson, G.M.1    Padera, T.P.2    Garkavtsev, I.3    Shioda, T.4    Jain, R.K.5
  • 59
    • 0034810699 scopus 로고    scopus 로고
    • Semaphorin 4C, a transmembrane semaphorin, [corrected] associates with a neurite-outgrowth-related protein, SFAP75
    • Ohoka, Y., M. Hirotani, H. Sugimoto, S. Fujioka, T. Furuyama, and S. Inagaki. 2001. Semaphorin 4C, a transmembrane semaphorin, [corrected] associates with a neurite-outgrowth-related protein, SFAP75. Biochem. Biophys. Res. Commun. 280:237-243. http://dx.doi.org/10.1006/bbrc.2000.4080
    • (2001) Biochem. Biophys. Res. Commun , vol.280 , pp. 237-243
    • Ohoka, Y.1    Hirotani, M.2    Sugimoto, H.3    Fujioka, S.4    Furuyama, T.5    Inagaki, S.6
  • 60
    • 33845472291 scopus 로고    scopus 로고
    • Scrib controls Cdc42 localization and activity to promote cell polarization during astrocyte migration
    • Osmani, N., N. Vitale, J.P. Borg, and S. Etienne-Manneville. 2006. Scrib controls Cdc42 localization and activity to promote cell polarization during astrocyte migration. Curr. Biol. 16:2395-2405. http://dx.doi.org/10.1016/j.cub.2006.10.026
    • (2006) Curr. Biol , vol.16 , pp. 2395-2405
    • Osmani, N.1    Vitale, N.2    Borg, J.P.3    Etienne-Manneville, S.4
  • 61
    • 84884397574 scopus 로고    scopus 로고
    • Dendritic cell migration through the lymphatic vasculature to lymph nodes
    • Platt, A.M., and G.J. Randolph. 2013. Dendritic cell migration through the lymphatic vasculature to lymph nodes. Adv. Immunol. 120:51-68 http://dx.doi/org/10.1016/B978-0-12-417028-5.00002-8.
    • (2013) Adv. Immunol , vol.120 , pp. 51-68
    • Platt, A.M.1    Randolph, G.J.2
  • 62
    • 0345731237 scopus 로고    scopus 로고
    • Cell migration: Rho GTPases lead the way
    • Raftopoulou, M., and A. Hall. 2004. Cell migration: Rho GTPases lead the way. Dev. Biol. 265:23-32. http://dx.doi.org/10.1016/j.ydbio.2003.06.003
    • (2004) Dev. Biol , vol.265 , pp. 23-32
    • Raftopoulou, M.1    Hall, A.2
  • 63
    • 23444451916 scopus 로고    scopus 로고
    • Dendritic-cell trafficking to lymph nodes through lymphatic vessels
    • Randolph, G.J., V. Angeli, and M.A. Swartz. 2005. Dendritic-cell trafficking to lymph nodes through lymphatic vessels. Nat. Rev. Immunol. 5:617-628. http://dx.doi.org/10.1038/nri1670
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 617-628
    • Randolph, G.J.1    Angeli, V.2    Swartz, M.A.3
  • 64
    • 42649091089 scopus 로고    scopus 로고
    • Migration of dendritic cell subsets and their precursors
    • Randolph, G.J., J. Ochando, and S. Partida-Sánchez. 2008. Migration of dendritic cell subsets and their precursors. Annu. Rev. Immunol. 26:293-316. http://dx.doi.org/10.1146/annurev.immunol.26.021607.090254
    • (2008) Annu. Rev. Immunol , vol.26 , pp. 293-316
    • Randolph, G.J.1    Ochando, J.2    Partida-Sánchez, S.3
  • 65
    • 0033777071 scopus 로고    scopus 로고
    • Determination of GTP loading on Rho
    • Ren, X.D., and M.A. Schwartz. 2000. Determination of GTP loading on Rho. Methods Enzymol. 325:264-272. http://dx.doi.org/10.1016/S0076-6879(00)25448-7
    • (2000) Methods Enzymol , vol.325 , pp. 264-272
    • Ren, X.D.1    Schwartz, M.A.2
  • 66
    • 84941283246 scopus 로고    scopus 로고
    • Rho GTPase signaling in cell migration
    • Ridley, A.J. 2015. Rho GTPase signaling in cell migration. Curr. Opin. Cell Biol. 36:103-112. http://dx.doi.org/10.1016/j.ceb.2015.08.005
    • (2015) Curr. Opin. Cell Biol , vol.36 , pp. 103-112
    • Ridley, A.J.1
  • 67
    • 84872363405 scopus 로고    scopus 로고
    • Immune plexins and semaphorins: Old proteins, new immune functions
    • Roney, K., E. Holl, and J. Ting. 2013. Immune plexins and semaphorins: old proteins, new immune functions. Protein Cell. 4:17-26. http://dx.doi.org/10.1007/s13238-012-2108-4
    • (2013) Protein Cell , vol.4 , pp. 17-26
    • Roney, K.1    Holl, E.2    Ting, J.3
  • 68
    • 84884478000 scopus 로고    scopus 로고
    • Dendritic cell interactions with lymphatic endothelium
    • Russo, E., M. Nitschké, and C. Halin. 2013. Dendritic cell interactions with lymphatic endothelium. Lymphat. Res. Biol. 11:172-182. http://dx.doi.org/10.1089/lrb.2013.0008
    • (2013) Lymphat. Res. Biol , vol.11 , pp. 172-182
    • Russo, E.1    Nitschké, M.2    Halin, C.3
  • 69
    • 84908424942 scopus 로고    scopus 로고
    • Rho GTPases: Masters of cell migration
    • Sadok, A., and C.J. Marshall. 2014. Rho GTPases: masters of cell migration. Small GTPases. 5. http://dx.doi.org/10.4161/sgtp.29710
    • (2014) Small GTPases , pp. 5
    • Sadok, A.1    Marshall, C.J.2
  • 70
    • 79952352658 scopus 로고    scopus 로고
    • Dynamics of the Rho-family small GTPases in actin regulation and motility
    • Spiering, D., and L. Hodgson. 2011. Dynamics of the Rho-family small GTPases in actin regulation and motility. Cell Adhes. Migr. 5:170-180. http://dx.doi.org/10.4161/cam.5.2.14403
    • (2011) Cell Adhes. Migr , vol.5 , pp. 170-180
    • Spiering, D.1    Hodgson, L.2
  • 71
    • 0037014472 scopus 로고    scopus 로고
    • Plexin-B1 directly interacts with PDZ-RhoGEF/LARG to regulate RhoA and growth cone morphology
    • Swiercz, J.M., R. Kuner, J. Behrens, and S. Offermanns. 2002. Plexin-B1 directly interacts with PDZ-RhoGEF/LARG to regulate RhoA and growth cone morphology. Neuron. 35:51-63. http://dx.doi.org/10.1016/S0896-6273(02)00750-X
    • (2002) Neuron , vol.35 , pp. 51-63
    • Swiercz, J.M.1    Kuner, R.2    Behrens, J.3    Offermanns, S.4
  • 72
    • 38349167245 scopus 로고    scopus 로고
    • ErbB-2 and Met reciprocally regulate cellular signaling via plexin-B1
    • Swiercz, J.M., T. Worzfeld, and S. Offermanns. 2008. ErbB-2 and Met reciprocally regulate cellular signaling via plexin-B1. J. Biol. Chem. 283:1893-1901. http://dx.doi.org/10.1074/jbc.M706822200
    • (2008) J. Biol. Chem , vol.283 , pp. 1893-1901
    • Swiercz, J.M.1    Worzfeld, T.2    Offermanns, S.3
  • 73
    • 84857686973 scopus 로고    scopus 로고
    • Diverse roles for semaphorin-plexin signaling in the immune system
    • Takamatsu, H., and A. Kumanogoh. 2012. Diverse roles for semaphorin-plexin signaling in the immune system. Trends Immunol. 33:127-135. http://dx.doi.org/10.1016/j.it.2012.01.008
    • (2012) Trends Immunol , vol.33 , pp. 127-135
    • Takamatsu, H.1    Kumanogoh, A.2
  • 74
    • 20244364929 scopus 로고    scopus 로고
    • Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates
    • Tamagnone, L., S. Artigiani, H. Chen, Z. He, G.I. Ming, H. Song, A. Chedotal, M.L. Winberg, C.S. Goodman, M. Poo, et al. 1999. Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates. Cell. 99:71-80. http://dx.doi.org/10.1016/S0092-8674(00)80063-X
    • (1999) Cell , vol.99 , pp. 71-80
    • Tamagnone, L.1    Artigiani, S.2    Chen, H.3    He, Z.4    Ming, G.I.5    Song, H.6    Chedotal, A.7    Winberg, M.L.8    Goodman, C.S.9    Poo, M.10
  • 75
    • 84899991702 scopus 로고    scopus 로고
    • Taking the lymphatic route: Dendritic cell migration to draining lymph nodes
    • Teijeira, A., E. Russo, and C. Halin. 2014. Taking the lymphatic route: dendritic cell migration to draining lymph nodes. Semin. Immunopathol. 36:261-274. http://dx.doi.org/10.1007/s00281-013-0410-8
    • (2014) Semin. Immunopathol , vol.36 , pp. 261-274
    • Teijeira, A.1    Russo, E.2    Halin, C.3
  • 76
    • 79955789504 scopus 로고    scopus 로고
    • Control of synapse development and plasticity by Rho GTPase regulatory proteins
    • Tolias, K.F., J.G. Duman, and K. Um. 2011. Control of synapse development and plasticity by Rho GTPase regulatory proteins. Prog. Neurobiol. 94:133-148. http://dx.doi.org/10.1016/j.pneurobio.2011.04.011
    • (2011) Prog. Neurobiol , vol.94 , pp. 133-148
    • Tolias, K.F.1    Duman, J.G.2    Um, K.3
  • 77
    • 0033553468 scopus 로고    scopus 로고
    • A PDZ protein regulates the distribution of the transmembrane semaphorin, M-SemF
    • Wang, L.H., R.G. Kalb, and S.M. Strittmatter. 1999. A PDZ protein regulates the distribution of the transmembrane semaphorin, M-SemF. J. Biol. Chem. 274:14137-14146. http://dx.doi.org/10.1074/jbc.274.20.14137
    • (1999) J. Biol. Chem , vol.274 , pp. 14137-14146
    • Wang, L.H.1    Kalb, R.G.2    Strittmatter, S.M.3
  • 78
    • 0035383772 scopus 로고    scopus 로고
    • Functional soluble CD100/Sema4D released from activated lymphocytes: Possible role in normal and pathologic immune responses
    • Wang, X., A. Kumanogoh, C. Watanabe, W. Shi, K. Yoshida, and H. Kikutani. 2001. Functional soluble CD100/Sema4D released from activated lymphocytes: possible role in normal and pathologic immune responses. Blood. 97:3498-3504. http://dx.doi.org/10.1182/blood.V97.11.3498
    • (2001) Blood , vol.97 , pp. 3498-3504
    • Wang, X.1    Kumanogoh, A.2    Watanabe, C.3    Shi, W.4    Yoshida, K.5    Kikutani, H.6
  • 79
    • 84886859740 scopus 로고    scopus 로고
    • Live cell imaging of chemotactic dendritic cell migration in explanted mouse ear preparations
    • Weber, M., and M. Sixt. 2013. Live cell imaging of chemotactic dendritic cell migration in explanted mouse ear preparations. Methods Mol. Biol. 1013:215-226. http://dx.doi.org/10.1007/978-1-62703-426-514
    • (2013) Methods Mol. Biol , vol.1013 , pp. 215-226
    • Weber, M.1    Sixt, M.2
  • 82
    • 84919723196 scopus 로고    scopus 로고
    • 3-acetylcholine receptor-G-protein-coupled receptor kinase 2 interaction
    • 3-acetylcholine receptor-G-protein-coupled receptor kinase 2 interaction. Mol. Pharmacol. 87:9-17. http://dx.doi.org/10.1124/mol.114.094722
    • (2015) Mol. Pharmacol , vol.87 , pp. 9-17
    • Wolters, V.1    Krasel, C.2    Brockmann, J.3    Bünemann, M.4
  • 83
    • 84905394859 scopus 로고    scopus 로고
    • Semaphorins and plexins as therapeutic targets
    • Worzfeld, T., and S. Offermanns. 2014. Semaphorins and plexins as therapeutic targets. Nat. Rev. Drug Discov. 13:603-621. http://dx.doi.org/10.1038/nrd4337
    • (2014) Nat. Rev. Drug Discov , vol.13 , pp. 603-621
    • Worzfeld, T.1    Offermanns, S.2
  • 86
    • 33746567767 scopus 로고    scopus 로고
    • The semaphorins
    • Yazdani, U., and J.R. Terman. 2006. The semaphorins. Genome Biol. 7. http://dx.doi.org/10.1186/gb-2006-7-3-211
    • (2006) Genome Biol , pp. 7
    • Yazdani, U.1    Terman, J.R.2
  • 87
    • 77956572619 scopus 로고    scopus 로고
    • Plexin A-semaphorin-1a reverse signaling regulates photoreceptor axon guidance in Drosophila
    • Yu, L., Y. Zhou, S. Cheng, and Y. Rao. 2010. Plexin A-semaphorin-1a reverse signaling regulates photoreceptor axon guidance in Drosophila. J. Neurosci. 30:12151-12156. http://dx.doi.org/10.1523/JNEUROSCI.1494-10.2010
    • (2010) J. Neurosci , vol.30 , pp. 12151-12156
    • Yu, L.1    Zhou, Y.2    Cheng, S.3    Rao, Y.4
  • 89
    • 77953254875 scopus 로고    scopus 로고
    • Recycling domains in plant cell morphogenesis: Small GTPase effectors, plasma membrane signalling and the exocyst
    • Žárský, V., and M. Potocký. 2010. Recycling domains in plant cell morphogenesis: small GTPase effectors, plasma membrane signalling and the exocyst. Biochem. Soc. Trans. 38:723-728. http://dx.doi.org/10.1042/BST0380723
    • (2010) Biochem. Soc. Trans , vol.38 , pp. 723-728
    • Žárský, V.1    Potocký, M.2
  • 90
    • 84922235046 scopus 로고    scopus 로고
    • Rho GTPases in collective cell migration
    • Zegers, M.M., and P. Friedl. 2014. Rho GTPases in collective cell migration. Small GTPases. 5. http://dx.doi.org/10.4161/sgtp.28997
    • (2014) Small GTPases , pp. 5
    • Zegers, M.M.1    Friedl, P.2


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