메뉴 건너뛰기




Volumn 4, Issue 8, 2003, Pages 651-657

Transactivation joins multiple tracks to the ERK/MAPK cascade

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANGIOTENSIN; BOMBESIN; BRADYKININ; CARBACHOL; ENDOTHELIN; ENDOTHELIN 1; EPIDERMAL GROWTH FACTOR RECEPTOR; G PROTEIN COUPLED RECEPTOR; INTEGRIN; LIGAND; LYSOPHOSPHATIDIC ACID; MITOGEN ACTIVATED PROTEIN KINASE; PHENYLEPHRINE; PHORBOL ESTER; SOMATOMEDIN C; THROMBIN;

EID: 0043172403     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1173     Document Type: Review
Times cited : (322)

References (63)
  • 1
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 103, 211-225 (2000)
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 3
    • 0028176297 scopus 로고
    • cAMP and βγ7 subunits of heterotrimeric G proteins stimulate the mitogen-activated protein kinase pathway in COS-7 cells
    • Faure, M., Voyno-Yasenetskaya, T. A. & Bourne, H. R. cAMP and βγ7 subunits of heterotrimeric G proteins stimulate the mitogen-activated protein kinase pathway in COS-7 cells. J. Biol. Chem. 269, 7851-7854 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 7851-7854
    • Faure, M.1    Voyno-Yasenetskaya, T.A.2    Bourne, H.R.3
  • 4
    • 0029790979 scopus 로고    scopus 로고
    • Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents
    • Knebel, A., Rahmsdorf, H. J., Ullrich, A. & Herdich, P. Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents. EMBO J. 15, 5314-5325 (1996).
    • (1996) EMBO J. , vol.15 , pp. 5314-5325
    • Knebel, A.1    Rahmsdorf, H.J.2    Ullrich, A.3    Herdich, P.4
  • 6
    • 0030044360 scopus 로고    scopus 로고
    • A Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors
    • Daub, H., Weiss, F. U., Wallasch, C. & Ullrich. A Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors. Nature 379, 557-560 (1996).
    • (1996) Nature , vol.379 , pp. 557-560
    • Daub, H.1    Weiss, F.U.2    Wallasch, C.3    Ullrich4
  • 7
    • 0034636685 scopus 로고    scopus 로고
    • Regulation of mitogen-activated protein kinase signaling networks by G protein-coupled receptors
    • Gutkind, J. S. Regulation of mitogen-activated protein kinase signaling networks by G protein-coupled receptors. Sci. STKE 2000. re1 (2000).
    • (2000) Sci. STKE , vol.2000
    • Gutkind, J.S.1
  • 8
    • 0035952741 scopus 로고    scopus 로고
    • Ras-MAP kinase signaling by lysophosphatidic acid and other G protein-coupled receptor agonists
    • Kranenburg, O. & Moolenaar, W. H. Ras-MAP kinase signaling by lysophosphatidic acid and other G protein-coupled receptor agonists. Oncogene 20, 1540-1546 (2001).
    • (2001) Oncogene , vol.20 , pp. 1540-1546
    • Kranenburg, O.1    Moolenaar, W.H.2
  • 9
    • 0035952645 scopus 로고    scopus 로고
    • New mechanisms in heptahelical receptor signaling to mitogen activated protein kinase cascades
    • Pierce, K. L., Luttrell, L. M. & Lefkowitz, R. J. New mechanisms in heptahelical receptor signaling to mitogen activated protein kinase cascades. Oncogene 20, 1532-1539 (2001).
    • (2001) Oncogene , vol.20 , pp. 1532-1539
    • Pierce, K.L.1    Luttrell, L.M.2    Lefkowitz, R.J.3
  • 10
    • 0035952656 scopus 로고    scopus 로고
    • Cell communication networks: Epidermal growth factor receptor transactivation as the paradigm for interreceptor signal transmission
    • Gschwind, A., Zwick, E., Prenzel, N., Leserer M. & Ullrich, A. Cell communication networks: epidermal growth factor receptor transactivation as the paradigm for interreceptor signal transmission. Oncogene 20, 1594-1600 (2001).
    • (2001) Oncogene , vol.20 , pp. 1594-1600
    • Gschwind, A.1    Zwick, E.2    Prenzel, N.3    Leserer, M.4    Ullrich, A.5
  • 11
    • 0036371753 scopus 로고    scopus 로고
    • Integration of signals from receptor tyrosine kinases and G protein-coupled receptors
    • Lowes, V. L., Ip, N. Y. & Wong, Y. H. Integration of signals from receptor tyrosine kinases and G protein-coupled receptors. Neurosignals 11, 5-19 (2002)
    • (2002) Neurosignals , vol.11 , pp. 5-19
    • Lowes, V.L.1    Ip, N.Y.2    Wong, Y.H.3
  • 12
    • 0034681203 scopus 로고    scopus 로고
    • EGF receptor transactivation mediated by the proteolytic production of EGF-like agonists
    • Carpenter, G. EGF receptor transactivation mediated by the proteolytic production of EGF-like agonists. Sci. STKE 2000, pe1 (2000).
    • (2000) Sci. STKE , vol.2000
    • Carpenter, G.1
  • 13
    • 0030683639 scopus 로고    scopus 로고
    • Signal characteristics of G protein-transactivated EGF receptor
    • Daub, H., Wallasch, C. Lankenau, A., Herdich, A. & Ullrich, A. Signal characteristics of G protein-transactivated EGF receptor. EMBO J. 16, 7032-7044 (1997).
    • (1997) EMBO J. , vol.16 , pp. 7032-7044
    • Daub, H.1    Wallasch, C.2    Lankenau, A.3    Herdich, A.4    Ullrich, A.5
  • 14
    • 0036152858 scopus 로고    scopus 로고
    • Cardiac hypertrophy is inhibited by antagonism of ADAM 12 processing of HB-EGF: Metalloproteinase inhibitors as a new therapy
    • Asakura, M. et al. Cardiac hypertrophy is inhibited by antagonism of ADAM 12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy. Nature Med. 8, 35-40 (2002).
    • (2002) Nature Med. , vol.8 , pp. 35-40
    • Asakura, M.1
  • 15
    • 0036828287 scopus 로고    scopus 로고
    • Lysophosphatidic acid-induced squamous cell carcinoma cell proliferation and motility involves epidermal growth factor receptor signal transactivation
    • Gschwind, A., Prenzel, N., & Ullrich, A. Lysophosphatidic acid-induced squamous cell carcinoma cell proliferation and motility involves epidermal growth factor receptor signal transactivation. Cancer Res. 62. 6329-6336 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 6329-6336
    • Gschwind, A.1    Prenzel, N.2    Ullrich, A.3
  • 16
    • 0036006453 scopus 로고    scopus 로고
    • Prostaglandin E2 transactivates EGF receptor: A novel mechanism for promoting colon cancer growth and gastrointestinal hypertrophy
    • Pai, R. et al. Prostaglandin E2 transactivates EGF receptor: a novel mechanism for promoting colon cancer growth and gastrointestinal hypertrophy. Nature Med. 8, 289-293 (2002).
    • (2002) Nature Med. , vol.8 , pp. 289-293
    • Pai, R.1
  • 17
    • 0035933814 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF) receptor-dependent ERK activation by G-protein-coupled receptors: A co-culture system for identifying intermediates upstream and downstream of heparin-binding EGF shedding
    • Pierce, K. L. et al. Epidermal growth factor (EGF) receptor-dependent ERK activation by G-protein-coupled receptors: a co-culture system for identifying intermediates upstream and downstream of heparin-binding EGF shedding. J. Biol. Chem. 276, 23155-23160 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 23155-23160
    • Pierce, K.L.1
  • 18
    • 0035910614 scopus 로고    scopus 로고
    • Angiotensin AT(1) and AT(2) receptors differentially regulate angiopoietin-2 and vascular endothelial growth factor expression and angiogenesis by modulating heparin binding-epidermal growth factor (EGF)-mediated EGF receptor transactivation
    • Fujiyama, S. et al. Angiotensin AT(1) and AT(2) receptors differentially regulate angiopoietin-2 and vascular endothelial growth factor expression and angiogenesis by modulating heparin binding-epidermal growth factor (EGF)-mediated EGF receptor transactivation. Circ. Res. 88, 22-29 (2001).
    • (2001) Circ. Res. , vol.88 , pp. 22-29
    • Fujiyama, S.1
  • 19
    • 0036313948 scopus 로고    scopus 로고
    • Helicobacter pylori-stimulated EGF receptor transactivation requires metalloprotease cleavage of HB-EGF
    • Wallasch, C. et al. Helicobacter pylori-stimulated EGF receptor transactivation requires metalloprotease cleavage of HB-EGF. Biochem. Biophys. Res. Commun. 295,695-701 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 695-701
    • Wallasch, C.1
  • 20
    • 0032815618 scopus 로고    scopus 로고
    • Radiation-induced release of transforming growth factor α activates the epidermal growth factor receptor and mitogen-activated protein kinase pathway in carcinoma cells, leading to increased proliferation and protection from radiation-induced cell death
    • Dent, P. et al. Radiation-induced release of transforming growth factor α activates the epidermal growth factor receptor and mitogen-activated protein kinase pathway in carcinoma cells, leading to increased proliferation and protection from radiation-induced cell death. Mol. Biol. Cell 10, 2493-2506 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2493-2506
    • Dent, P.1
  • 21
    • 0033599039 scopus 로고    scopus 로고
    • EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
    • Prenzel, N. et al. EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature 402, 884-888 (1999).
    • (1999) Nature , vol.402 , pp. 884-888
    • Prenzel, N.1
  • 22
    • 0029778177 scopus 로고    scopus 로고
    • βγ subunit-mediated activation of mitogen-activated protein kinases
    • βγ subunit-mediated activation of mitogen-activated protein kinases. J. Biol. Chem. 271, 19443-19450 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 19443-19450
    • Luttrell, L.M.1
  • 23
    • 0033583220 scopus 로고    scopus 로고
    • c-Src-mediated phosphorylation of the epidermal growth factor receptor on Tyr 845 and Tyr1101 is associated with modulation of receptor function
    • Biscardi, J. S. et al. c-Src-mediated phosphorylation of the epidermal growth factor receptor on Tyr845 and Tyr1101 is associated with modulation of receptor function. J. Biol. Chem. 274, 8335-8343 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 8335-8343
    • Biscardi, J.S.1
  • 25
    • 0037085234 scopus 로고    scopus 로고
    • New members of the platelet-derived growth factor family of mitogens
    • Heldin, C. H., Eriksson, U. & Ostman, A. New members of the platelet-derived growth factor family of mitogens. Arch. Biochem. Biophys. 398, 284-290 (2002).
    • (2002) Arch. Biochem. Biophys. , vol.398 , pp. 284-290
    • Heldin, C.H.1    Eriksson, U.2    Ostman, A.3
  • 26
    • 0028805435 scopus 로고
    • Thrombin stimulates phosphorylation of insulin-like growth factor-1 receptor, insulin receptor substrate-1, and phospholipase C-γ-1 in rat aortic smooth muscle cells
    • Rao, G. N., Delafontaine, P & Runge, M. S. Thrombin stimulates phosphorylation of insulin-like growth factor-1 receptor, insulin receptor substrate-1, and phospholipase C-γ-1 in rat aortic smooth muscle cells. J. Biol. Chem. 270, 27871-27875 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 27871-27875
    • Rao, G.N.1    Delafontaine, P.2    Runge, M.S.3
  • 27
    • 0035853065 scopus 로고    scopus 로고
    • Activation of Trk neurotrophin receptors in the absence of neurotrophins
    • Lee, F. S. & Chao, M. V. Activation of Trk neurotrophin receptors in the absence of neurotrophins. Proc. Natl Acad. Sci. USA. 98, 3555-3560 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3555-3560
    • Lee, F.S.1    Chao, M.V.2
  • 28
    • 0036317107 scopus 로고    scopus 로고
    • Integrative nuclear FGFR1 signaling (INFS) pathway mediates activation of the tyrosine hydroxylase gene by angiotensin II, depolarization and protein kinase C
    • Peng, H. et al. Integrative nuclear FGFR1 signaling (INFS) pathway mediates activation of the tyrosine hydroxylase gene by angiotensin II, depolarization and protein kinase C. J. Neurochem. 81, 506-524 (2002).
    • (2002) J. Neurochem. , vol.81 , pp. 506-524
    • Peng, H.1
  • 29
    • 0035371620 scopus 로고    scopus 로고
    • Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases
    • Östman, A. & Bohmer, F. D. Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases. Trends Cell. Biol 11, 258-266 (2001).
    • (2001) Trends Cell. Biol. , vol.11 , pp. 258-266
    • Östman, A.1    Bohmer, F.D.2
  • 30
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng, T. C., Fukada, T. & Tonks, N. K. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9, 387-399 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 32
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation
    • Rhee, S. G., Bae, Y. S., Lee, S. R. & Kwon, J. Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation. Sci. STKE 2000, pe1 (2000).
    • (2000) Sci. STKE , vol.2000
    • Rhee, S.G.1    Bae, Y.S.2    Lee, S.R.3    Kwon, J.4
  • 33
    • 0028806450 scopus 로고
    • Participation of reactive oxygen species in the lysophosphatidic acid-stimulated mitogen-activated protein kinase kinase activation pathway
    • Chen, Q., Olashaw, N. & Wu, J. Participation of reactive oxygen species in the lysophosphatidic acid-stimulated mitogen-activated protein kinase kinase activation pathway. J. Biol. Chem. 270, 28499-28502 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 28499-28502
    • Chen, Q.1    Olashaw, N.2    Wu, J.3
  • 34
    • 0033538516 scopus 로고    scopus 로고
    • Stimulation of a vascular smooth muscle cell NAD(P)H oxidase by thrombin. Evidence that p47(phox) may participate in forming this oxidase in vitro and in vivo
    • Patterson, C. et al. Stimulation of a vascular smooth muscle cell NAD(P)H oxidase by thrombin. Evidence that p47(phox) may participate in forming this oxidase in vitro and in vivo. J. Biol. Chem. 274, 19814-19822 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 19814-19822
    • Patterson, C.1
  • 35
    • 0034807142 scopus 로고    scopus 로고
    • Regulation of MAP kinase activity by peptide receptor signalling pathway: Paradigms of multiplicity
    • Liebmann, C. Regulation of MAP kinase activity by peptide receptor signalling pathway: paradigms of multiplicity. Cell. Signal. 13, 777-785 (2001).
    • (2001) Cell. Signal. , vol.13 , pp. 777-785
    • Liebmann, C.1
  • 36
    • 0031037296 scopus 로고    scopus 로고
    • Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase γ
    • Lopez-Ilasaca, M., Crespo, P., Pellici, P. G., Gutkind, J. S. & Wetzker, R. Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase γ. Science 275, 394-397 (1997).
    • (1997) Science , vol.275 , pp. 394-397
    • Lopez-Ilasaca, M.1    Crespo, P.2    Pellici, P.G.3    Gutkind, J.S.4    Wetzker, R.5
  • 37
    • 0034682836 scopus 로고    scopus 로고
    • β2-adrenergic receptor activates extracellular signal-regulated kinases (ERKs) via the small G protein rap1 and the serine/threonine kinase B-Raf
    • Schmitt, J. M. & Stork, P. J. β2-adrenergic receptor activates extracellular signal-regulated kinases (ERKs) via the small G protein rap1 and the serine/threonine kinase B-Raf. J. Biol. Chem. 275, 25342-25350 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 25342-25350
    • Schmitt, J.M.1    Stork, P.J.2
  • 38
    • 0035827528 scopus 로고    scopus 로고
    • Src and Pyk2 mediate G-protein-coupled receptor activation of epidermal growth factor receptor (EGFR) but are not required for coupling to the mitogen-activated protein (MAP) kinase signaling cascade
    • Andreev, J. et al. Src and Pyk2 mediate G-protein-coupled receptor activation of epidermal growth factor receptor (EGFR) but are not required for coupling to the mitogen-activated protein (MAP) kinase signaling cascade. J. Biol. Chem. 276, 20130-20135 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 20130-20135
    • Andreev, J.1
  • 39
    • 0037077201 scopus 로고    scopus 로고
    • A function for phosphoinositide 3-kinase lipid products in coupling βγ to Ras activation in response to lysophosphatidic acid
    • Yart, A. et al. A function for phosphoinositide 3-kinase lipid products in coupling βγ to Ras activation in response to lysophosphatidic acid. J. Biol. Chem. 277, 21167-21178 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 21167-21178
    • Yart, A.1
  • 40
    • 0033553526 scopus 로고    scopus 로고
    • Pleiotropic coupling of G protein-coupled receptors to the mitogen-activated protein kinase cascade. Role of focal adhesions and receptor tyrosine kinases
    • Della Rocca, G. J., Maudsley, S., Daaka, Y., Lefkowitz, R. J. & Luttrell, L. M. Pleiotropic coupling of G protein-coupled receptors to the mitogen-activated protein kinase cascade. Role of focal adhesions and receptor tyrosine kinases. J. Biol. Chem. 274, 13978-13984 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 13978-13984
    • Della Rocca, G.J.1    Maudsley, S.2    Daaka, Y.3    Lefkowitz, R.J.4    Luttrell, L.M.5
  • 41
    • 0032808149 scopus 로고    scopus 로고
    • Bradykinin B(2) receptor-mediated mitogen-activated protein kinase activation in COS-7 cells requires dual signaling via both protein kinase C pathway and epidermal growth factor receptor transactivation
    • Adomeit, A. et al. Bradykinin B(2) receptor-mediated mitogen-activated protein kinase activation in COS-7 cells requires dual signaling via both protein kinase C pathway and epidermal growth factor receptor transactivation. Mol. Cell. Biol. 19, 5289-5297 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5289-5297
    • Adomeit, A.1
  • 42
    • 0037144657 scopus 로고    scopus 로고
    • Protease-activated receptor-1-mediated DNA synthesis in cardiac fibroblast is via epidermal growth factor receptor transactivation: Distinct PAR-1 signaling pathways in cardiac fibroblasts and cardiomyocytes
    • Sabri, A., Short, J., Guo, J. & Steinberg, S. F. Protease-activated receptor-1-mediated DNA synthesis in cardiac fibroblast is via epidermal growth factor receptor transactivation: distinct PAR-1 signaling pathways in cardiac fibroblasts and cardiomyocytes. Circ. Res. 91, 532-539 (2002).
    • (2002) Circ. Res. , vol.91 , pp. 532-539
    • Sabri, A.1    Short, J.2    Guo, J.3    Steinberg, S.F.4
  • 43
    • 0036847024 scopus 로고    scopus 로고
    • Inducible gene deletion reveals different roles for B-Raf and Raf-1 in B-cell antigen receptor signalling
    • Brummer, T., Shaw, P. E., Reth, M. & Misawa, Y. Inducible gene deletion reveals different roles for B-Raf and Raf-1 in B-cell antigen receptor signalling EMBO J. 21, 5611-5622 (2002).
    • (2002) EMBO J. , vol.21 , pp. 5611-5622
    • Brummer, T.1    Shaw, P.E.2    Reth, M.3    Misawa, Y.4
  • 44
    • 0035204534 scopus 로고    scopus 로고
    • Cross talk between β-adrenergic and bradykinin B(2) receptors results in cooperative regulation of cyclic AMP accumulation and mitogen-activated protein kinase activity
    • Hanke, S., Nürnberg, B., Groll, D. H. & Liebmann, C. Cross talk between β-adrenergic and bradykinin B(2) receptors results in cooperative regulation of cyclic AMP accumulation and mitogen-activated protein kinase activity. Mol. Cell. Biol. 21, 8452-8460 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8452-8460
    • Hanke, S.1    Nürnberg, B.2    Groll, D.H.3    Liebmann, C.4
  • 45
    • 0037900130 scopus 로고    scopus 로고
    • Mechanisms of protease-activated receptor-4 actions in cardiomyocytes: Role of Src tyrosine kinase
    • Sabri, A. et al. Mechanisms of protease-activated receptor-4 actions in cardiomyocytes: role of Src tyrosine kinase. J. Biol. Chem. 278, 11714-11720 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 11714-11720
    • Sabri, A.1
  • 46
    • 0037341631 scopus 로고    scopus 로고
    • Spontaneous receptor-independent heterotrimeric G-protein signalling in an RGS mutant
    • Siekhaus, D. E. & Drubin, D. G. Spontaneous receptor-independent heterotrimeric G-protein signalling in an RGS mutant. Nature Cell. Biol. 5, 231-235 (2003).
    • (2003) Nature Cell. Biol. , vol.5 , pp. 231-235
    • Siekhaus, D.E.1    Drubin, D.G.2
  • 47
    • 0033013866 scopus 로고    scopus 로고
    • Role of phosphoinositide 3-kinase in activation of ras and mitogen-activated protein kinase by epidermal growth factor
    • Wennström, S. & Downward, J. Role of phosphoinositide 3-kinase in activation of ras and mitogen-activated protein kinase by epidermal growth factor. Mol. Cell Biol. 19, 4279-4288 (1999).
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4279-4288
    • Wennström, S.1    Downward, J.2
  • 48
    • 0034609756 scopus 로고    scopus 로고
    • A permissive function of phosphoinositide 3-kinase in Ras activation mediated by inhibition of GTPase-activating proteins
    • Rubio, I. & Wetzker, R. A permissive function of phosphoinositide 3-kinase in Ras activation mediated by inhibition of GTPase-activating proteins. Curr. Biol. 10, 1225-1228 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 1225-1228
    • Rubio, I.1    Wetzker, R.2
  • 49
    • 0037470136 scopus 로고    scopus 로고
    • Cholecystokinin stimulates extracellular signal-regulated kinase through activation of the epidermal growth factor receptor, Yes, and protein kinase C. Signal amplification at the level of Raf by activation of protein kinase Cε
    • Piiper, A. et al. Cholecystokinin stimulates extracellular signal-regulated kinase through activation of the epidermal growth factor receptor, Yes, and protein kinase C. Signal amplification at the level of Raf by activation of protein kinase Cε. J. Biol. Chem. 278, 7065-7072 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 7065-7072
    • Piiper, A.1
  • 50
    • 0037127297 scopus 로고    scopus 로고
    • Rapid transactivation of the vascular endothelial growth factor receptor KDR/Flk-1 by the bradykinin B2 receptor contributes to endothelial nitric-oxide synthase activation in cardiac capillary endothelial cells
    • Thuringer, D., Maulon, L. & Frelin, C. Rapid transactivation of the vascular endothelial growth factor receptor KDR/Flk-1 by the bradykinin B2 receptor contributes to endothelial nitric-oxide synthase activation in cardiac capillary endothelial cells. J. Biol. Chem. 277, 2028-2032 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 2028-2032
    • Thuringer, D.1    Maulon, L.2    Frelin, C.3
  • 51
    • 0037008761 scopus 로고    scopus 로고
    • Activation of BAD by therapeutic inhibition of epidermal growth factor receptor and transactivation by insulin-like growth factor receptor
    • Gilmore, A. P. et al. Activation of BAD by therapeutic inhibition of epidermal growth factor receptor and transactivation by insulin-like growth factor receptor. J. Biol. Chem. 277, 27643-27650 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 27643-27650
    • Gilmore, A.P.1
  • 52
    • 0030770603 scopus 로고    scopus 로고
    • Critical role of calcium-dependent epidermal growth factor receptor transactivation in PC 12 cell membrane depolarization and bradykinin signaling
    • Zwick, E. et al. Critical role of calcium-dependent epidermal growth factor receptor transactivation in PC 12 cell membrane depolarization and bradykinin signaling. J. Biol. Chem. 272, 24767-24770 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 24767-24770
    • Zwick, E.1
  • 53
    • 0032538798 scopus 로고    scopus 로고
    • Integrins induce activation of EGF receptor: Role in MAP kinase induction and adhesion-dependent cell survival
    • Moro, L. et al. Integrins induce activation of EGF receptor: role in MAP kinase induction and adhesion-dependent cell survival. EMBO J. 17, 6622-6632 (1998).
    • (1998) EMBO J. , vol.17 , pp. 6622-6632
    • Moro, L.1
  • 54
    • 0035861689 scopus 로고    scopus 로고
    • Transactivation of the epidermal growth factor receptor is involved in 12-O-tetradecanoylphorbol-13-acetate-induced signal transduction
    • Chen, N. et al. Transactivation of the epidermal growth factor receptor is involved in 12-O-tetradecanoylphorbol-13-acetate-induced signal transduction. J. Biol. Chem. 276, 46722-46728 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 46722-46728
    • Chen, N.1
  • 55
    • 0030034469 scopus 로고    scopus 로고
    • G-protein coupled and tyrosine kinase receptors: Evidence that activation of the insulin-like growth factor I receptor is required for thrombin-induced mitogenesis of rat aortic smooth muscle cells
    • Delafontaine, P., Anwar, A., Lou, H. & Ku, L. G-protein coupled and tyrosine kinase receptors: evidence that activation of the insulin-like growth factor I receptor is required for thrombin-induced mitogenesis of rat aortic smooth muscle cells. J. Clin. Invest. 97, 139-145 (1996).
    • (1996) J. Clin. Invest. , vol.97 , pp. 139-145
    • Delafontaine, P.1    Anwar, A.2    Lou, H.3    Ku, L.4
  • 56
    • 0032555202 scopus 로고    scopus 로고
    • Ligand-independent activation of platelet-derived growth factor receptor is a necessary intermediate in lysophosphatidic acid-stimulated mitogenic activity in L cells
    • Herrlich, A. et al. Ligand-independent activation of platelet-derived growth factor receptor is a necessary intermediate in lysophosphatidic acid-stimulated mitogenic activity in L cells. Proc. Natl Acad. Sci. USA 95, 8985-8990 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8985-8990
    • Herrlich, A.1
  • 57
    • 0029074408 scopus 로고
    • Convergence of angiotensin II and platelet-derived growth factor receptor signaling cascades in vascular smooth muscle cells
    • Linseman, D. A., Benjamin, C. W. & Jones, D. A. Convergence of angiotensin II and platelet-derived growth factor receptor signaling cascades in vascular smooth muscle cells. J. Biol. Chem. 270, 12563-12568 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 12563-12568
    • Linseman, D.A.1    Benjamin, C.W.2    Jones, D.A.3
  • 58
    • 0034520154 scopus 로고    scopus 로고
    • Tumor necrosis factor-α converting enzyme (TACE) is a growth hormone binding protein (GHBP) sheddase: The metalloprotease TACE/ADAM-17 is critical for (PMA-induced) GH receptor proteolysis and GHBP generation
    • Zhang, Y., Jiang, J., Black, R. A., Baumann, G. & Frank, S. J. Tumor necrosis factor-α converting enzyme (TACE) is a growth hormone binding protein (GHBP) sheddase: the metalloprotease TACE/ADAM-17 is critical for (PMA-induced) GH receptor proteolysis and GHBP generation. Endocrinology 141, 4342-4348 (2000).
    • (2000) Endocrinology , vol.141 , pp. 4342-4348
    • Zhang, Y.1    Jiang, J.2    Black, R.A.3    Baumann, G.4    Frank, S.J.5
  • 59
    • 0037157854 scopus 로고    scopus 로고
    • The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors
    • Yan, Y., Shirakabe, K. & Werb, Z. The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors. J. Cell. Biol. 158, 221-226 (2002).
    • (2002) J. Cell. Biol. , vol.158 , pp. 221-226
    • Yan, Y.1    Shirakabe, K.2    Werb, Z.3
  • 60
    • 0036152681 scopus 로고    scopus 로고
    • Platelet-activating factor receptor and ADAM 10 mediate responses to Staphylococcus aureus in epithelial cells
    • Lemjabbar, H. & Basbaum, C. Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells. Nature Med. 8, 41-46 (2002).
    • (2002) Nature Med. , vol.8 , pp. 41-46
    • Lemjabbar, H.1    Basbaum, C.2
  • 61
    • 0038581051 scopus 로고    scopus 로고
    • TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells
    • Gschwind, A. Hart, S. Fischer, O. M. & Ullrich, A. TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells. EMBO J. 22, 2411-2421 (2003).
    • (2003) EMBO J. , vol.22 , pp. 2411-2421
    • Gschwind, A.1    Hart, S.2    Fischer, O.M.3    Ullrich, A.4
  • 62
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen et al. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423, 769-773 (2003).
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen1
  • 63
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort, R. L., Congreve, M., Tisi, D., Carr, R. & Jhoti, H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 423, 773-777 (2003).
    • (2003) Nature , vol.423 , pp. 773-777
    • Van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.