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Volumn 15, Issue 5, 2003, Pages 565-571

Interactions between growth factor receptors and adhesion molecules: Breaking the rules

Author keywords

[No Author keywords available]

Indexed keywords

CADHERIN; CELL ADHESION MOLECULE; GROWTH FACTOR; INTEGRIN;

EID: 0141756154     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(03)00096-6     Document Type: Review
Times cited : (217)

References (49)
  • 1
    • 0036775137 scopus 로고    scopus 로고
    • Integrin signaling: It's where the action is
    • Damsky C.H., Ilic D. Integrin signaling: it's where the action is. Curr Opin Cell Biol. 14:2002;594-602.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 594-602
    • Damsky, C.H.1    Ilic, D.2
  • 2
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk
    • Geiger B., Bershadsky A., Pankov R., Yamada K.M. Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk. Nat Rev Mol Cell Biol. 2:2001;793-805.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 3
  • 4
    • 0036222549 scopus 로고    scopus 로고
    • Sensing the environment: A historical perspective on integrin signal transduction
    • Miranti C.K., Brugge J.S. Sensing the environment: a historical perspective on integrin signal transduction. Nat Cell Biol. 4:2002;83-90.
    • (2002) Nat Cell Biol , vol.4 , pp. 83-90
    • Miranti, C.K.1    Brugge, J.S.2
  • 5
    • 0036229695 scopus 로고    scopus 로고
    • Integrin regulation of growth factor receptors
    • Yamada K.M., Even-Ram S. Integrin regulation of growth factor receptors. Nat Cell Biol. 4:2002;E75-E76.
    • (2002) Nat Cell Biol , vol.4
    • Yamada, K.M.1    Even-Ram, S.2
  • 6
    • 0036229694 scopus 로고    scopus 로고
    • Networks and crosstalk: Integrin signalling spreads
    • Schwartz M.A., Ginsberg M.H. Networks and crosstalk: integrin signalling spreads. Nat Cell Biol. 4:2002;E65-E68.
    • (2002) Nat Cell Biol , vol.4
    • Schwartz, M.A.1    Ginsberg, M.H.2
  • 7
    • 0034671718 scopus 로고    scopus 로고
    • Cell adhesion regulates ubiquitin-mediated degradation of the platelet-derived growth factor receptor β
    • Baron V., Schwartz M. Cell adhesion regulates ubiquitin-mediated degradation of the platelet-derived growth factor receptor β J Biol Chem. 275:2000;39318-39323.
    • (2000) J Biol Chem , vol.275 , pp. 39318-39323
    • Baron, V.1    Schwartz, M.2
  • 8
    • 0030814976 scopus 로고    scopus 로고
    • αvβ3 integrin associates with activated insulin and PDGFβ receptors and potentiates the biological activity of PDGF
    • Schneller M., Vuori K., Ruoslahti E. αvβ3 integrin associates with activated insulin and PDGFβ receptors and potentiates the biological activity of PDGF. EMBO J. 16:1997;5600-5607.
    • (1997) EMBO J , vol.16 , pp. 5600-5607
    • Schneller, M.1    Vuori, K.2    Ruoslahti, E.3
  • 9
    • 0034704174 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor β and vascular endothelial growth factor receptor 2 bind to the β3 integrin through its extracellular domain
    • Borgest E., Jan Y., Ruoslahti E. Platelet-derived growth factor receptor β and vascular endothelial growth factor receptor 2 bind to the β3 integrin through its extracellular domain. J Biol Chem. 275:2000;39867-39873.
    • (2000) J Biol Chem , vol.275 , pp. 39867-39873
    • Borgest, E.1    Jan, Y.2    Ruoslahti, E.3
  • 10
    • 0033558087 scopus 로고    scopus 로고
    • Role of αvβ3 integrin in the activation of vascular endothelial growth factor receptor-2
    • Soldi R., Mitola S., Strasly M., Defilippi P., Tarone G., Bussolino F. Role of αvβ3 integrin in the activation of vascular endothelial growth factor receptor-2. EMBO J. 18:1999;882-892.
    • (1999) EMBO J , vol.18 , pp. 882-892
    • Soldi, R.1    Mitola, S.2    Strasly, M.3    Defilippi, P.4    Tarone, G.5    Bussolino, F.6
  • 12
    • 0036826862 scopus 로고    scopus 로고
    • The αvβ3 integrin regulates insulin-like growth factor (IGF-I) receptor phosphorylation by altering the rate of recruitment of the Src-homology 2-containing phosphotyrosine phosphatase-2 to the activated IGF-I receptor
    • This paper describes one of the possible mechanisms whereby αvβ3-mediated adhesion results in enhanced signalling from the insulin-like growth factor-1 (IGF-1) receptor. When αvβ3 is prevented from ligand occupancy by the disintegrin echistatin, the IGF-1 receptor directly recruits the tyrosine phosphatase Shp2, which in turn reduces the phosphorylation levels of the receptor.
    • Maile L.A., Clemmons D.R. The αvβ3 integrin regulates insulin-like growth factor (IGF-I) receptor phosphorylation by altering the rate of recruitment of the Src-homology 2-containing phosphotyrosine phosphatase-2 to the activated IGF-I receptor. Endocrinology. 143: 2002;4259-4264 This paper describes one of the possible mechanisms whereby αvβ3-mediated adhesion results in enhanced signalling from the insulin-like growth factor-1 (IGF-1) receptor. When αvβ3 is prevented from ligand occupancy by the disintegrin echistatin, the IGF-1 receptor directly recruits the tyrosine phosphatase Shp2, which in turn reduces the phosphorylation levels of the receptor.
    • (2002) Endocrinology , vol.143 , pp. 4259-4264
    • Maile, L.A.1    Clemmons, D.R.2
  • 15
    • 0036850183 scopus 로고    scopus 로고
    • CNS integrins switch growth factor signalling to promote target-dependent survival
    • •]) shows that interactions between integrins and growth factor receptors, together with integrin engagement by axonal ligands, drive the developmental stages of oligodendrocyte maturation. In oligodendrocyte progenitors, platelet-derived growth factor (PDGF)-dependent mitogenic activity requires association of the PDGF receptor with αvβ3 integrin, which leads to PDGF-induced, protein-kinase-C-dependent activation of αvβ3, mediated by an increase in the affinity for matrix ligands. In turn, integrin activation results in the stimulation of an adhesion-dependent phosphatidylinositol 3-kinase pathway that promotes oligodendrocyte proliferation. During the transition from progenitor cell to mature cell, oligodendrocytes require survival signals provided by the integration of short-range cues from the extracellular matrix with long-range growth factor signals.
    • •]) shows that interactions between integrins and growth factor receptors, together with integrin engagement by axonal ligands, drive the developmental stages of oligodendrocyte maturation. In oligodendrocyte progenitors, platelet-derived growth factor (PDGF)-dependent mitogenic activity requires association of the PDGF receptor with αvβ3 integrin, which leads to PDGF-induced, protein-kinase-C-dependent activation of αvβ3, mediated by an increase in the affinity for matrix ligands. In turn, integrin activation results in the stimulation of an adhesion-dependent phosphatidylinositol 3-kinase pathway that promotes oligodendrocyte proliferation. During the transition from progenitor cell to mature cell, oligodendrocytes require survival signals provided by the integration of short-range cues from the extracellular matrix with long-range growth factor signals. Specifically, when oligodendrocytes locally contact axonal laminins through α6β1, they begin mounting a survival response following stimulation with diffusible neuregulin, PDGF, or subliminal concentration of both.
    • (2002) Nat Cell Biol , vol.4 , pp. 833-841
    • Colognato, H.1    Baron, W.2    Avellana-Adalid, V.3    Relvas, J.B.4    Evercooren, A.B.-V.5    Georges-Labouesse, E.6    French-Constant, C.7
  • 18
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P., Hunter T. Oncogenic kinase signalling. Nature. 411:2001;355-365.
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 19
    • 0032538798 scopus 로고    scopus 로고
    • Integrins induce activation of EGF receptor: Role in MAPK induction and adhesion-dependent cell survival
    • Moro L., Venturino M., Bozzo C., Silengo L., Altruda F., Beguinot L., Tarone G., Defilippi P. Integrins induce activation of EGF receptor: role in MAPK induction and adhesion-dependent cell survival. EMBO J. 17:1998;6622-6632.
    • (1998) EMBO J , vol.17 , pp. 6622-6632
    • Moro, L.1    Venturino, M.2    Bozzo, C.3    Silengo, L.4    Altruda, F.5    Beguinot, L.6    Tarone, G.7    Defilippi, P.8
  • 20
    • 0033623969 scopus 로고    scopus 로고
    • Integrin α5/β1 mediates fibronectin-dependent epithelial cell proliferation through epidermal growth factor receptor activation
    • Kuwada S.K., Li X. Integrin α5/β1 mediates fibronectin-dependent epithelial cell proliferation through epidermal growth factor receptor activation. Mol Biol Cell. 11:2000;2485-2496.
    • (2000) Mol Biol Cell , vol.11 , pp. 2485-2496
    • Kuwada, S.K.1    Li, X.2
  • 21
    • 0029670904 scopus 로고    scopus 로고
    • Stimulation of β1 integrins on fibroblasts induces PDGF-independent tyrosine phosphorylation of PDGF β receptors
    • Sundberg C., Rubin K. Stimulation of β1 integrins on fibroblasts induces PDGF-independent tyrosine phosphorylation of PDGF β receptors. J Cell Biol. 132:1996;741-752.
    • (1996) J Cell Biol , vol.132 , pp. 741-752
    • Sundberg, C.1    Rubin, K.2
  • 22
    • 0035834793 scopus 로고    scopus 로고
    • Stimulation of β1 integrin induces tyrosine phosphorylation of vascular endothelial growth factor receptor-3 and modulates cell migration
    • Wang J.F., Zhang X.-F., Groopman J.E. Stimulation of β1 integrin induces tyrosine phosphorylation of vascular endothelial growth factor receptor-3 and modulates cell migration. J Biol Chem. 276:2001;41950-41957.
    • (2001) J Biol Chem , vol.276 , pp. 41950-41957
    • Wang, J.F.1    Zhang, X.-F.2    Groopman, J.E.3
  • 23
    • 0029759716 scopus 로고    scopus 로고
    • Cellular adherence elicits ligand-independent activation of the Met cell-surface receptor
    • Wang R., Kobayashi R., Bishop J.M. Cellular adherence elicits ligand-independent activation of the Met cell-surface receptor. Proc Natl Acad Sci USA. 93:1996;8425-8430.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8425-8430
    • Wang, R.1    Kobayashi, R.2    Bishop, J.M.3
  • 24
    • 0035947770 scopus 로고    scopus 로고
    • Activation of the Met receptor by cell attachment induces and sustains hepatocellular carcinomas in transgenic mice
    • This is the first in vivo demonstration that transgenic expression of wild-type Met in hepatocytes of mice results in adhesion-dependent, hepatocyte-growth-factor-independent activation of the receptor, leading to development of hepatocellular carcinomas. Transgene inactivation is followed by regression of even highly advanced tumours.
    • Wang R., Ferrell L.D., Faouzi S., Maher J.J., Bishop J.M. Activation of the Met receptor by cell attachment induces and sustains hepatocellular carcinomas in transgenic mice. J Cell Biol. 153:2001;1023-1034 This is the first in vivo demonstration that transgenic expression of wild-type Met in hepatocytes of mice results in adhesion-dependent, hepatocyte-growth-factor-independent activation of the receptor, leading to development of hepatocellular carcinomas. Transgene inactivation is followed by regression of even highly advanced tumours.
    • (2001) J Cell Biol , vol.153 , pp. 1023-1034
    • Wang, R.1    Ferrell, L.D.2    Faouzi, S.3    Maher, J.J.4    Bishop, J.M.5
  • 25
    • 0034686013 scopus 로고    scopus 로고
    • Integrin-mediated RON growth factor receptor phosphorylation requires tyrosine kinase activity of both the receptor and c-Src
    • Danilkovitch-Miagkova A., Angeloni D., Skeel A., Donley S., Lerman M., Leonard E.J. Integrin-mediated RON growth factor receptor phosphorylation requires tyrosine kinase activity of both the receptor and c-Src. J Biol Chem. 275:2000;14783-14786.
    • (2000) J Biol Chem , vol.275 , pp. 14783-14786
    • Danilkovitch-Miagkova, A.1    Angeloni, D.2    Skeel, A.3    Donley, S.4    Lerman, M.5    Leonard, E.J.6
  • 26
    • 0033947684 scopus 로고    scopus 로고
    • Integrin α2β1-dependent EGF receptor activation at cell-cell contact sites
    • Yu X., Miyamoto S., Mekada E. Integrin α2β1-dependent EGF receptor activation at cell-cell contact sites. J Cell Sci. 113:2000;2139-2147.
    • (2000) J Cell Sci , vol.113 , pp. 2139-2147
    • Yu, X.1    Miyamoto, S.2    Mekada, E.3
  • 27
    • 0037088647 scopus 로고    scopus 로고
    • Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines
    • This paper provides an accurate biochemical dissection of the molecular mechanisms regulating integrin-dependent epidermal growth factor (EGF) receptor phosphorylation. Cell adhesion leads to activation of c-Src and to c-Src-dependent recruitment of EGF receptors and p130Cas in a macromolecular complex. c-Src catalytic activity is also required for EGF receptor phosphorylation and activation. The pattern of receptor phosphorylation following cell adhesion is different from that induced by soluble EGF: specifically, Tyr1148, a key residue normally phosphorylated after EGF stimulation, remains unphosphorylated upon integrin ligation. Furthermore, while Tyr845 on the receptor is likely to be directly phosphorylated by Src, phosphorylation of the other residues requires kinase activity from the receptor itself.
    • Moro L., Dolce L., Cabodi S., Bergatto E., Boeri Erba E., Smeriglio M., Turco E., Retta S.F., Giuffrida M.G., Venturino M.et al. Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines. J Biol Chem. 277:2002;9405-9414 This paper provides an accurate biochemical dissection of the molecular mechanisms regulating integrin-dependent epidermal growth factor (EGF) receptor phosphorylation. Cell adhesion leads to activation of c-Src and to c-Src-dependent recruitment of EGF receptors and p130Cas in a macromolecular complex. c-Src catalytic activity is also required for EGF receptor phosphorylation and activation. The pattern of receptor phosphorylation following cell adhesion is different from that induced by soluble EGF: specifically, Tyr1148, a key residue normally phosphorylated after EGF stimulation, remains unphosphorylated upon integrin ligation. Furthermore, while Tyr845 on the receptor is likely to be directly phosphorylated by Src, phosphorylation of the other residues requires kinase activity from the receptor itself.
    • (2002) J Biol Chem , vol.277 , pp. 9405-9414
    • Moro, L.1    Dolce, L.2    Cabodi, S.3    Bergatto, E.4    Boeri Erba, E.5    Smeriglio, M.6    Turco, E.7    Retta, S.F.8    Giuffrida, M.G.9    Venturino, M.10
  • 28
    • 0035479918 scopus 로고    scopus 로고
    • The α6β4 integrin and epithelial cell migration
    • An equanimous and highly informative review on the many, and often contradictory, aspects of α6β4-dependent signals and biological effects.
    • Mercurio A.M., Rabinovitz I., Shaw L.M. The α6β4 integrin and epithelial cell migration. Curr Opin Cell Biol. 13:2001;541-545 An equanimous and highly informative review on the many, and often contradictory, aspects of α6β4-dependent signals and biological effects.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 541-545
    • Mercurio, A.M.1    Rabinovitz, I.2    Shaw, L.M.3
  • 29
    • 0032908323 scopus 로고    scopus 로고
    • Structure and function of hemidesmosomes: More than simple adhesion complexes
    • Borradori L., Sonnenberg A. Structure and function of hemidesmosomes: more than simple adhesion complexes. J Invest Dermatol. 112:1999;411-418.
    • (1999) J Invest Dermatol , vol.112 , pp. 411-418
    • Borradori, L.1    Sonnenberg, A.2
  • 30
    • 0031283128 scopus 로고    scopus 로고
    • The integrin α6β4 functions in carcinoma cell migration on laminin-1 by mediating the formation and stabilization of actin-containing motility structures
    • Rabinovitz I., Mercurio A.M. The integrin α6β4 functions in carcinoma cell migration on laminin-1 by mediating the formation and stabilization of actin-containing motility structures. J Cell Biol. 139:1997;1873-1884.
    • (1997) J Cell Biol , vol.139 , pp. 1873-1884
    • Rabinovitz, I.1    Mercurio, A.M.2
  • 31
    • 0034707597 scopus 로고    scopus 로고
    • RhoA function in lamellae formation and migration is regulated by the α6β4 integrin and cAMP metabolism
    • O'Connor K.L., Nguyen B.K., Mercurio A.M. RhoA function in lamellae formation and migration is regulated by the α6β4 integrin and cAMP metabolism. J Cell Biol. 148:2000;253-258.
    • (2000) J Cell Biol , vol.148 , pp. 253-258
    • O'Connor, K.L.1    Nguyen, B.K.2    Mercurio, A.M.3
  • 32
    • 0035851913 scopus 로고    scopus 로고
    • EGF-R signaling through Fyn kinase disrupts the function of integrin α6β4 at hemidesmosomes: Role in epithelial cell migration and carcinoma invasion
    • This paper shows that an epidermal growth factor (EGF)-triggered signalling complex consisting of the EGF receptor, the cytosolic tyrosine kinase Fyn and the α6β4 integrin promotes hemidesmosome disassembly in epithelial cells and stimulates cell invasion. This is accomplished through EGF-receptor-dependent activation of Fyn, which in turn phosphorylates the β4 cytoplasmic domain. Expression of dominant-negative Fyn isoforms in carcinoma cells increases hemidesmosome formation, impairs EGF-dependent migration in vitro, and reduces lung metastases following intravenous injection in nude mice.
    • Mariotti A., Kedeshian P.A., Dans M., Curatola A.M., Gagnoux-Palacios L., Giancotti F.G. EGF-R signaling through Fyn kinase disrupts the function of integrin α6β4 at hemidesmosomes: role in epithelial cell migration and carcinoma invasion. J Cell Biol. 155:2001;447-458 This paper shows that an epidermal growth factor (EGF)-triggered signalling complex consisting of the EGF receptor, the cytosolic tyrosine kinase Fyn and the α6β4 integrin promotes hemidesmosome disassembly in epithelial cells and stimulates cell invasion. This is accomplished through EGF-receptor-dependent activation of Fyn, which in turn phosphorylates the β4 cytoplasmic domain. Expression of dominant-negative Fyn isoforms in carcinoma cells increases hemidesmosome formation, impairs EGF-dependent migration in vitro, and reduces lung metastases following intravenous injection in nude mice.
    • (2001) J Cell Biol , vol.155 , pp. 447-458
    • Mariotti, A.1    Kedeshian, P.A.2    Dans, M.3    Curatola, A.M.4    Gagnoux-Palacios, L.5    Giancotti, F.G.6
  • 33
    • 0032845770 scopus 로고    scopus 로고
    • Protein kinase C-dependent mobilization of the α6β4 integrin from hemidesmosomes and its association with actin-rich cell protrusions drive the chemotactic migration of carcinoma cells
    • Rabinovitz I., Toker A., Mercurio A.M. Protein kinase C-dependent mobilization of the α6β4 integrin from hemidesmosomes and its association with actin-rich cell protrusions drive the chemotactic migration of carcinoma cells. J Cell Biol. 146:1999;1147-1160.
    • (1999) J Cell Biol , vol.146 , pp. 1147-1160
    • Rabinovitz, I.1    Toker, A.2    Mercurio, A.M.3
  • 34
    • 0031456065 scopus 로고    scopus 로고
    • Activation of phosphoinositide 3-OH kinase by the α6β4 integrin promotes carcinoma invasion
    • Shaw L.M., Rabinovitz I., Wang H.H., Toker A., Mercurio A.M. Activation of phosphoinositide 3-OH kinase by the α6β4 integrin promotes carcinoma invasion. Cell. 91:1997;949-960.
    • (1997) Cell , vol.91 , pp. 949-960
    • Shaw, L.M.1    Rabinovitz, I.2    Wang, H.H.3    Toker, A.4    Mercurio, A.M.5
  • 35
    • 0034615933 scopus 로고    scopus 로고
    • Cooperative signaling between α6β4 integrin and ErbB-2 receptor is required to promote phosphatidylinositol 3-kinase-dependent invasion
    • Gambaletta D., Marchetti A., Benedetti L., Mercurio A.M., Sacchi A., Falcioni R. Cooperative signaling between α6β4 integrin and ErbB-2 receptor is required to promote phosphatidylinositol 3-kinase-dependent invasion. J Biol Chem. 275:2000;10604-10610.
    • (2000) J Biol Chem , vol.275 , pp. 10604-10610
    • Gambaletta, D.1    Marchetti, A.2    Benedetti, L.3    Mercurio, A.M.4    Sacchi, A.5    Falcioni, R.6
  • 36
    • 0035977147 scopus 로고    scopus 로고
    • A signaling adapter function for α6β4 integrin in the control of HGF-dependent invasive growth
    • This is the first demonstration that an integrin can act as a functional signalling molecule without engagement of its extracellular ligand-binding domain. In various tumour cell lines, integrin α6β4 complexes with the hepatocyte growth factor (HGF) receptor Met. Following Met activation, β4 gets tyrosine-phosphorylated and recruits Shc and phosphatidylinositol 3-kinase, thus acting as a docking molecule to activate further downstream signalling events and potentiate HGF-dependent cell invasion. The same adaptor function is accomplished by a truncated variant of β4 unable to bind laminins.
    • Trusolino L., Bertotti A., Comoglio P.M. A signaling adapter function for α6β4 integrin in the control of HGF-dependent invasive growth. Cell. 107:2001;643-654 This is the first demonstration that an integrin can act as a functional signalling molecule without engagement of its extracellular ligand-binding domain. In various tumour cell lines, integrin α6β4 complexes with the hepatocyte growth factor (HGF) receptor Met. Following Met activation, β4 gets tyrosine-phosphorylated and recruits Shc and phosphatidylinositol 3-kinase, thus acting as a docking molecule to activate further downstream signalling events and potentiate HGF-dependent cell invasion. The same adaptor function is accomplished by a truncated variant of β4 unable to bind laminins.
    • (2001) Cell , vol.107 , pp. 643-654
    • Trusolino, L.1    Bertotti, A.2    Comoglio, P.M.3
  • 38
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark E.A., Brugge J.S. Integrins and signal transduction pathways: the road taken. Science. 268:1995;233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 39
    • 0037421188 scopus 로고    scopus 로고
    • Direct cadherin-activated cell signaling: A view from the plasma membrane
    • Yap A.S., Kovacs E.M. Direct cadherin-activated cell signaling: a view from the plasma membrane. J Cell Biol. 160:2003;11-16.
    • (2003) J Cell Biol , vol.160 , pp. 11-16
    • Yap, A.S.1    Kovacs, E.M.2
  • 40
    • 0037459077 scopus 로고    scopus 로고
    • Sticky business: Orchestrating cellular signals at adherens junctions
    • Perez-Moreno M., Jamora C., Fuchs E. Sticky business: orchestrating cellular signals at adherens junctions. Cell. 112:2003;535-548.
    • (2003) Cell , vol.112 , pp. 535-548
    • Perez-Moreno, M.1    Jamora, C.2    Fuchs, E.3
  • 42
    • 0037047090 scopus 로고    scopus 로고
    • VEGF receptor 2 and the adherens junction as a mechanical transducer in vascular endothelial cells
    • This paper shows for the first time that endothelial cells sense shear stress through a multimolecular complex consisting of vascular endothelial growth factor (VEGF) receptor-2, VE-cadherin and β-catenin. Shear stress stimulates induction and nuclear translocation of VEGF receptor-2, as well as its association with VE-cadherin and β-catenin at cell-cell adhesion sites. In endothelial cells lacking VE-cadherin, shear stress does not promote nuclear translocation of VEGF receptor and does not induce transcription of a reporter gene under the control of a shear-stress-responsive promoter.
    • Shay-Salit A., Shushy M., Wolfovitz E., Yahav H., Breviario F., Dejana E., Resnick N. VEGF receptor 2 and the adherens junction as a mechanical transducer in vascular endothelial cells. Proc Natl Acad Sci USA. 99:2002;9462-9467 This paper shows for the first time that endothelial cells sense shear stress through a multimolecular complex consisting of vascular endothelial growth factor (VEGF) receptor-2, VE-cadherin and β-catenin. Shear stress stimulates induction and nuclear translocation of VEGF receptor-2, as well as its association with VE-cadherin and β-catenin at cell-cell adhesion sites. In endothelial cells lacking VE-cadherin, shear stress does not promote nuclear translocation of VEGF receptor and does not induce transcription of a reporter gene under the control of a shear-stress-responsive promoter.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9462-9467
    • Shay-Salit, A.1    Shushy, M.2    Wolfovitz, E.3    Yahav, H.4    Breviario, F.5    Dejana, E.6    Resnick, N.7
  • 43
    • 0034945537 scopus 로고    scopus 로고
    • N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling
    • This paper provides an insightful analysis of the signalling mechanisms underlying the pro-adhesive function of N-CAM in β cells from pancreatic tumours. N-CAM stimulates β1-integrin-dependent matrix adhesion by assembling a huge multimolecular complex comprising, among others, N-cadherin, fibroblast growth factor receptor (FGFR) 4, and phospholipase Cγ. Dominant-negative variants of FGFR-4, inhibitors of FGFR-4 signalling, and function-blocking antibodies against β1 integrins impair NCAM-induced adhesion.
    • Cavallaro U., Niedermeyer J., Fuxa M., Christofori G. N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling. Nat Cell Biol. 3:2001;650-657 This paper provides an insightful analysis of the signalling mechanisms underlying the pro-adhesive function of N-CAM in β cells from pancreatic tumours. N-CAM stimulates β1-integrin-dependent matrix adhesion by assembling a huge multimolecular complex comprising, among others, N-cadherin, fibroblast growth factor receptor (FGFR) 4, and phospholipase Cγ. Dominant-negative variants of FGFR-4, inhibitors of FGFR-4 signalling, and function-blocking antibodies against β1 integrins impair NCAM-induced adhesion.
    • (2001) Nat Cell Biol , vol.3 , pp. 650-657
    • Cavallaro, U.1    Niedermeyer, J.2    Fuxa, M.3    Christofori, G.4
  • 44
    • 0034731148 scopus 로고    scopus 로고
    • Signaling from E-cadherins to the MAPK pathway by the recruitment and activation of epidermal growth factor receptors upon cell-cell contact formation
    • Pece S., Gutkind J.S. Signaling from E-cadherins to the MAPK pathway by the recruitment and activation of epidermal growth factor receptors upon cell-cell contact formation. J Biol Chem. 275:2000;41227-41233.
    • (2000) J Biol Chem , vol.275 , pp. 41227-41233
    • Pece, S.1    Gutkind, J.S.2
  • 45
    • 0037020084 scopus 로고    scopus 로고
    • Rac activation upon cell-cell contact formation is dependent on signaling from the epidermal growth factor receptor
    • These papers (see also Pece and Gutkind [2000] [44]) provide two examples of intracellular signals triggered by intercellular adhesion as a consequence of ligand-independent activation of the epidermal growth factor (EGF) receptor. Formation of cell-cell contacts between neighbouring cells leads to association of E-cadherin to the EGF receptor, receptor transactivation, Shc phosphorylation and stimulation of mitogen-activated protein kinase (MAPK) activity. Moreover, induction of intercellular adhesion results in Rac activation, which can be blocked by pharmacological inhibitors of the EGF receptor, but not by inhibitors of phosphatidylinositol 3-kinase or MAPK.
    • Betson M., Lozano E., Zhang J., Braga V.M. Rac activation upon cell-cell contact formation is dependent on signaling from the epidermal growth factor receptor. J Biol Chem. 277:2002;36962-36969 These papers (see also Pece and Gutkind [2000] [44]) provide two examples of intracellular signals triggered by intercellular adhesion as a consequence of ligand-independent activation of the epidermal growth factor (EGF) receptor. Formation of cell-cell contacts between neighbouring cells leads to association of E-cadherin to the EGF receptor, receptor transactivation, Shc phosphorylation and stimulation of mitogen-activated protein kinase (MAPK) activity. Moreover, induction of intercellular adhesion results in Rac activation, which can be blocked by pharmacological inhibitors of the EGF receptor, but not by inhibitors of phosphatidylinositol 3-kinase or MAPK.
    • (2002) J Biol Chem , vol.277 , pp. 36962-36969
    • Betson, M.1    Lozano, E.2    Zhang, J.3    Braga, V.M.4
  • 46
    • 0028170977 scopus 로고
    • β-catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor
    • Hoschuetzky H., Aberle H., Kemler R. β-catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor. J Cell Biol. 127:1994;1375-1380.
    • (1994) J Cell Biol , vol.127 , pp. 1375-1380
    • Hoschuetzky, H.1    Aberle, H.2    Kemler, R.3
  • 47
    • 0031825437 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces VE-cadherin tyrosine phosphorylation in endothelial cells
    • Esser S., Lampugnani M.G., Corada M., Dejana E., Risau W. Vascular endothelial growth factor induces VE-cadherin tyrosine phosphorylation in endothelial cells. J Cell Sci. 111:1998;1853-1865.
    • (1998) J Cell Sci , vol.111 , pp. 1853-1865
    • Esser, S.1    Lampugnani, M.G.2    Corada, M.3    Dejana, E.4    Risau, W.5
  • 48
    • 0036118004 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces SHC association with vascular endothelial cadherin: A potential feedback mechanism to control vascular endothelial growth factor receptor-2 signaling
    • This is the first demonstration that vascular endothelial growth factor (VEGF)-dependent tyrosine phosphorylation of VE-cadherin results in cadherin association with Shc. Phosphorylation of Shc on VEGF stimulation lasts longer in endothelial cells lacking VE-cadherin than in cells expressing it, suggesting that VE-cadherin plays a negative role in Shc phosphorylation by the VEGF receptor-2.
    • Zanetti A., Lampugnani M.G., Balconi G., Breviario F., Corada M., Lanfrancone L., Dejana E. Vascular endothelial growth factor induces SHC association with vascular endothelial cadherin: a potential feedback mechanism to control vascular endothelial growth factor receptor-2 signaling. Arterioscler Thromb Vasc Biol. 22:2002;617-622 This is the first demonstration that vascular endothelial growth factor (VEGF)-dependent tyrosine phosphorylation of VE-cadherin results in cadherin association with Shc. Phosphorylation of Shc on VEGF stimulation lasts longer in endothelial cells lacking VE-cadherin than in cells expressing it, suggesting that VE-cadherin plays a negative role in Shc phosphorylation by the VEGF receptor-2.
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 617-622
    • Zanetti, A.1    Lampugnani, M.G.2    Balconi, G.3    Breviario, F.4    Corada, M.5    Lanfrancone, L.6    Dejana, E.7
  • 49
    • 0036121308 scopus 로고    scopus 로고
    • Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex
    • The authors report the identification a new E3 ubiquitin ligase, called Hakai, that specifically interacts with E-cadherin in its tyrosine-phosphorylated form. Hakai induces E2-dependent ubiquitination of the E-cadherin complex in vitro and in vivo and promotes endocytosis of the E-cadherin-catenin complex, thus relating the activity of tyrosine kinases at cell-cell contacts with the degradation of junctional components and the consequent impairment of intercellular adhesion.
    • Fujita Y., Krause G., Scheffner M., Zechner D., Leddy H.E., Behrens J., Sommer T., Birchmeier W. Hakai, a c-Cbl-like protein, ubiquitinates and induces endocytosis of the E-cadherin complex. Nat Cell Biol. 4:2002;222-231 The authors report the identification a new E3 ubiquitin ligase, called Hakai, that specifically interacts with E-cadherin in its tyrosine-phosphorylated form. Hakai induces E2-dependent ubiquitination of the E-cadherin complex in vitro and in vivo and promotes endocytosis of the E-cadherin-catenin complex, thus relating the activity of tyrosine kinases at cell-cell contacts with the degradation of junctional components and the consequent impairment of intercellular adhesion.
    • (2002) Nat Cell Biol , vol.4 , pp. 222-231
    • Fujita, Y.1    Krause, G.2    Scheffner, M.3    Zechner, D.4    Leddy, H.E.5    Behrens, J.6    Sommer, T.7    Birchmeier, W.8


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