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Volumn 247, Issue 3, 1997, Pages 1190-1196

Identification of an ubiquitin-ligation system for the epidermal-growth-factor receptor Herbimycin A induces in vitro ubiquitination in rabbit-reticulocyte lysate

Author keywords

Epidermal growth factor receptor; Herbimycin A; Ubiquitin conjugating enzyme; Ubiquitin protein ligase; Ubiquitination

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; HERBIMYCIN A; UBIQUITIN CONJUGATING ENZYME;

EID: 0030792186     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.01190.x     Document Type: Article
Times cited : (13)

References (29)
  • 2
    • 0028137446 scopus 로고
    • Signal transduction by the PDGF receptors
    • Claesson-Welsh, L. (1994) Signal transduction by the PDGF receptors, Prog. Growth Factor Res. 5, 37-54.
    • (1994) Prog. Growth Factor Res. , vol.5 , pp. 37-54
    • Claesson-Welsh, L.1
  • 3
    • 0025765803 scopus 로고
    • SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins
    • Koch, C. A., Anderson, D., Moran, M. F., Ellis, C. & Pawson, T. (1991) SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins, Science 252, 668-674.
    • (1991) Science , vol.252 , pp. 668-674
    • Koch, C.A.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 4
    • 0026664626 scopus 로고
    • Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor
    • Mori, S., Heldin, C.-H. & Claesson-Welsh, L. (1992) Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor, J. Biol. Chem. 267, 6429-6434.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6429-6434
    • Mori, S.1    Heldin, C.-H.2    Claesson-Welsh, L.3
  • 5
    • 0027402689 scopus 로고
    • Ligand-induced ubiquitination of the platelet-derived growth factor β-receptor plays a negative regulatory role in its mitogenic signaling
    • Mori, S., Heldin, C.-H. & Claesson-Welsh, L. (1993) Ligand-induced ubiquitination of the platelet-derived growth factor β-receptor plays a negative regulatory role in its mitogenic signaling, J. Biol. Chem. 268, 577-583.
    • (1993) J. Biol. Chem. , vol.268 , pp. 577-583
    • Mori, S.1    Heldin, C.-H.2    Claesson-Welsh, L.3
  • 7
    • 0028158499 scopus 로고
    • Ligand-dependent polyubiquitination of c-kit gene product: A possible mechanism of receptor down modulation in M07e cells
    • Miyazawa, K., Toyama, K., Gotoh, A., Hendrie, P. C., Mantel, C. & Broxmeyer, H. E. (1994) Ligand-dependent polyubiquitination of c-kit gene product: a possible mechanism of receptor down modulation in M07e cells, Blood 83, 137-145.
    • (1994) Blood , vol.83 , pp. 137-145
    • Miyazawa, K.1    Toyama, K.2    Gotoh, A.3    Hendrie, P.C.4    Mantel, C.5    Broxmeyer, H.E.6
  • 8
    • 0029557613 scopus 로고
    • The epidermal-growth-factor receptor is covalently linked to ubiquitin
    • Galcheva-Gargova, Z., Theroux, S. J. & Davis, R. J. (1995) The epidermal-growth-factor receptor is covalently linked to ubiquitin, Oncogene 11, 2649-2655.
    • (1995) Oncogene , vol.11 , pp. 2649-2655
    • Galcheva-Gargova, Z.1    Theroux, S.J.2    Davis, R.J.3
  • 9
    • 0028118679 scopus 로고
    • The ubiquitin-mediated proteolytic pathway: Mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins
    • Ciechanover, A. & Schwartz, A. L. (1994) The ubiquitin-mediated proteolytic pathway: mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins, FASEB J. 8, 182-191.
    • (1994) FASEB J. , vol.8 , pp. 182-191
    • Ciechanover, A.1    Schwartz, A.L.2
  • 10
    • 0025875671 scopus 로고
    • Natural substrates of the ubiquitin proteolytic pathway
    • Rechsteiner, M. (1991) Natural substrates of the ubiquitin proteolytic pathway, Cell 66, 615-618.
    • (1991) Cell , vol.66 , pp. 615-618
    • Rechsteiner, M.1
  • 11
    • 0025799525 scopus 로고
    • The ubiquitin pathway for protein degradation
    • Hershko, A. (1991) The ubiquitin pathway for protein degradation, Trends Biochem. Sci. 16, 265-268.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 265-268
    • Hershko, A.1
  • 13
  • 14
    • 0028788180 scopus 로고
    • Degradation process of ligand-stimulated platelet-derived growth factor β-receptor involves ubiquitin-proteasome proteolytic pathway
    • Mori, S., Tanaka, K., Omura, S. & Saito, Y. (1995) Degradation process of ligand-stimulated platelet-derived growth factor β-receptor involves ubiquitin-proteasome proteolytic pathway, J. Biol. Chem. 270, 29447-29452.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29447-29452
    • Mori, S.1    Tanaka, K.2    Omura, S.3    Saito, Y.4
  • 15
    • 0029587276 scopus 로고
    • Ligand-activated platelet-derived growth factor β-receptor is degraded through proteasome-dependent proteolytic pathway
    • Mori, S., Kanaki, H., Tanaka, K., Morisaki, N. & Saito, Y. (1995) Ligand-activated platelet-derived growth factor β-receptor is degraded through proteasome-dependent proteolytic pathway, Biochem. Biophys. Res. Commun. 217, 224-229.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 224-229
    • Mori, S.1    Kanaki, H.2    Tanaka, K.3    Morisaki, N.4    Saito, Y.5
  • 16
    • 0028304022 scopus 로고
    • Accelerated degradation of 160 kDa epidermal-growth-factor (EGF) receptor precursor by the tyrosine kinase inhibitor herbimycin A in the endoplasmic reticulim of A431 human epidermoid carcinoma cells
    • Murakami, Y., Mizuno, S. & Uehara, Y. (1994) Accelerated degradation of 160 kDa epidermal-growth-factor (EGF) receptor precursor by the tyrosine kinase inhibitor herbimycin A in the endoplasmic reticulim of A431 human epidermoid carcinoma cells, Biochem. J. 301, 63-68.
    • (1994) Biochem. J. , vol.301 , pp. 63-68
    • Murakami, Y.1    Mizuno, S.2    Uehara, Y.3
  • 17
    • 0029008487 scopus 로고
    • Herbimycin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases
    • Sepp-Lorenzino, L., Ma, Z., Lebwohl, D. E., Vinitsky, A. & Rosen, N. (1995) Herbimycin A induces the 20 S proteasome- and ubiquitin-dependent degradation of receptor tyrosine kinases, J. Biol. Chem. 270, 16580-16587.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16580-16587
    • Sepp-Lorenzino, L.1    Ma, Z.2    Lebwohl, D.E.3    Vinitsky, A.4    Rosen, N.5
  • 18
    • 0021932292 scopus 로고
    • Screening of agents which convert transformed morphology of Rous sarcoma virus-infected rat kidney cells to normal morphology: Identification of an active agent as herbimycin and its inhibition of intracellular src kinase
    • Uehara, Y., Hori, M., Takeuchi, T. & Umezawa, H. (1985) Screening of agents which convert transformed morphology of Rous sarcoma virus-infected rat kidney cells to normal morphology: identification of an active agent as herbimycin and its inhibition of intracellular src kinase, Jpn. J. Cancer Res. 76, 672-675.
    • (1985) Jpn. J. Cancer Res. , vol.76 , pp. 672-675
    • Uehara, Y.1    Hori, M.2    Takeuchi, T.3    Umezawa, H.4
  • 19
    • 0023940887 scopus 로고
    • Inhibition of transforming activity of tyrosine kinase oncogenes by herbimycin A
    • Uehara, Y., Murakami, Y., Mizuno, S. & Kawai, S. (1988) Inhibition of transforming activity of tyrosine kinase oncogenes by herbimycin A, Virology 164, 294-298.
    • (1988) Virology , vol.164 , pp. 294-298
    • Uehara, Y.1    Murakami, Y.2    Mizuno, S.3    Kawai, S.4
  • 20
    • 0024467122 scopus 로고
    • Irreversible inhibition of v-src tyrosine kinase activity by herbimycin A and its abrogation by sulfhydryl compounds
    • Uehara, Y., Fukazawa, H., Murakami, Y. & Mizuno, S. (1989) Irreversible inhibition of v-src tyrosine kinase activity by herbimycin A and its abrogation by sulfhydryl compounds, Biochem. Biophys. Res. Commun. 163, 803-809.
    • (1989) Biochem. Biophys. Res. Commun. , vol.163 , pp. 803-809
    • Uehara, Y.1    Fukazawa, H.2    Murakami, Y.3    Mizuno, S.4
  • 22
    • 0026458235 scopus 로고
    • Tyrphostins: Tyrosine kinase blockers as novel antiproliferative agents and dissectors of signal transduction
    • Levitzki, A. (1992) Tyrphostins: tyrosine kinase blockers as novel antiproliferative agents and dissectors of signal transduction, FASEB J. 6, 3275-3282.
    • (1992) FASEB J. , vol.6 , pp. 3275-3282
    • Levitzki, A.1
  • 23
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system: Resolution, affinity purification, and role in protein breakdown
    • Hershko, A., Heller, H., Elias, S. & Ciechanover, A. (1983) Components of ubiquitin-protein ligase system: resolution, affinity purification, and role in protein breakdown, J. Biol. Chem. 258, 8206-8214.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 24
    • 0025917982 scopus 로고
    • Improved method for preparation of ubiquitin-ligated lysozyme as substrate of ATP-dependent proleolysis
    • Tamura, T., Tanaka, K., Tanahashi, N. & Ichihara, A. (1991) Improved method for preparation of ubiquitin-ligated lysozyme as substrate of ATP-dependent proleolysis, FEBS Lett. 292, 154-158.
    • (1991) FEBS Lett. , vol.292 , pp. 154-158
    • Tamura, T.1    Tanaka, K.2    Tanahashi, N.3    Ichihara, A.4
  • 25
    • 0028939392 scopus 로고
    • Reconstitution of p53-ubiquitinylation reactions from purified components: The role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP)
    • Rolfe, M., Beer-Romero, P., Glass, S., Eckstein, J., Berdo, I., Theodoras, A., Pagano, M. & Draetta, G. (1995) Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP), Proc. Natl Acad. Sci. USA 92, 3264-3268.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3264-3268
    • Rolfe, M.1    Beer-Romero, P.2    Glass, S.3    Eckstein, J.4    Berdo, I.5    Theodoras, A.6    Pagano, M.7    Draetta, G.8
  • 26
    • 0028233372 scopus 로고
    • Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-N-end rule protein substrates
    • Blumenfeld, N., Gonen, H., Mayer, A., Smith, C. E., Siegel, N. R., Schwartz, A. L. & Ciechanover, A. (1994) Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-N-end rule protein substrates, J. Biol. Chem. 269, 9574-9581.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9574-9581
    • Blumenfeld, N.1    Gonen, H.2    Mayer, A.3    Smith, C.E.4    Siegel, N.R.5    Schwartz, A.L.6    Ciechanover, A.7
  • 27
    • 0028342731 scopus 로고
    • Complete reconstitution of conjugation and subsequent degradation of the tumor suppressor protein p53 by purified components of the ubiquitin proteolytic system
    • Shkedy, D., Gonen, H., Bercovich, B. & Ciechanover, A. (1994) Complete reconstitution of conjugation and subsequent degradation of the tumor suppressor protein p53 by purified components of the ubiquitin proteolytic system, FEBS Lett. 348, 126-130.
    • (1994) FEBS Lett. , vol.348 , pp. 126-130
    • Shkedy, D.1    Gonen, H.2    Bercovich, B.3    Ciechanover, A.4
  • 28
    • 0029812759 scopus 로고    scopus 로고
    • c-erbB2 receptor protein-tyrosine kinase induced by geldanamycin
    • c-erbB2 receptor protein-tyrosine kinase induced by geldanamycin, J. Biol. Chem. 271, 22796-22801.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3


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