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Volumn 139, Issue 4, 1997, Pages 995-1003

Constitutive proteolysis of the ErbB-4 receptor tyrosine kinase by a unique, sequential mechanism

Author keywords

[No Author keywords available]

Indexed keywords

METALLOPROTEINASE; NEU DIFFERENTIATION FACTOR; PROTEASOME; PROTEIN TYROSINE KINASE; RECEPTOR;

EID: 0030661989     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.4.995     Document Type: Article
Times cited : (114)

References (53)
  • 1
  • 2
    • 0025973804 scopus 로고
    • Ligand-independent activation of the sevenless receptor tyrosine kinase changes the fate of cells in the developing drosophila eye
    • Basler, K., B. Christen, and E. Hafen. 1991. Ligand-independent activation of the sevenless receptor tyrosine kinase changes the fate of cells in the developing drosophila eye. Cell. 64:1069-1081.
    • (1991) Cell , vol.64 , pp. 1069-1081
    • Basler, K.1    Christen, B.2    Hafen, E.3
  • 3
    • 0029912203 scopus 로고    scopus 로고
    • All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired
    • Baulida, J., M.H. Kraus, M. Alimandi, P.P. Di Fiore, and G. Carpenter. 1996. All ErbB receptors other than the epidermal growth factor receptor are endocytosis impaired. J. Biol. Chem. 271:5251-5257.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5251-5257
    • Baulida, J.1    Kraus, M.H.2    Alimandi, M.3    Di Fiore, P.P.4    Carpenter, G.5
  • 6
    • 0031010398 scopus 로고    scopus 로고
    • Covalent modification of the active site threonine of proteasomal β subunits and the Escherichia coli homologue HsIV by a new class of inhibitors
    • Bogyo, M., J.S. McMaster, M. Gaczynska, D. Tortorella, A.L. Goldberg, and H. Ploegh. 1997. Covalent modification of the active site threonine of proteasomal β subunits and the Escherichia coli homologue HsIV by a new class of inhibitors. Proc. Natl. Acad. Sci. USA. 94:6629-6634.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6629-6634
    • Bogyo, M.1    McMaster, J.S.2    Gaczynska, M.3    Tortorella, D.4    Goldberg, A.L.5    Ploegh, H.6
  • 7
    • 0028227722 scopus 로고
    • Protein kinase C-dependent release of a functional whole extracellular domain of the mast cell growth factor (MGF) receptor by MGF-dependent human myeloid cells
    • Brizzi, M.F., J.M. Blechman, G. Cavalloni, D. Givol, Y. Yarden, and L. Pegoraro. 1994. Protein kinase C-dependent release of a functional whole extracellular domain of the mast cell growth factor (MGF) receptor by MGF-dependent human myeloid cells. Oncogene. 9:1583-1589.
    • (1994) Oncogene , vol.9 , pp. 1583-1589
    • Brizzi, M.F.1    Blechman, J.M.2    Cavalloni, G.3    Givol, D.4    Yarden, Y.5    Pegoraro, L.6
  • 8
    • 0030020074 scopus 로고    scopus 로고
    • Trka receptor ectodomain cleavage generates a tyrosine-phosphorylated cell-associated fragment
    • Cabrera, N., E. Díaz-Rodríguez, E. Becker, D. Martín-Zanca, and A. Pandiella. 1996. TrkA receptor ectodomain cleavage generates a tyrosine-phosphorylated cell-associated fragment. J. Cell Biol. 132:427-436.
    • (1996) J. Cell Biol. , vol.132 , pp. 427-436
    • Cabrera, N.1    Díaz-Rodríguez, E.2    Becker, E.3    Martín-Zanca, D.4    Pandiella, A.5
  • 9
    • 0017103026 scopus 로고
    • 125I-labeled human epidermal growth factor. Binding, internalization, and degradation in human fibroblasts
    • 125I-labeled human epidermal growth factor. Binding, internalization, and degradation in human fibroblasts. J. Cell Biol. 71:159-171.
    • (1976) J. Cell Biol. , vol.71 , pp. 159-171
    • Carpenter, G.1    Cohen, S.2
  • 11
    • 0028323719 scopus 로고
    • Tissue-specific transformation by oncogenic mutants of epidermal growth factor receptor
    • Carter, T.H., and H.J. Kung. 1994. Tissue-specific transformation by oncogenic mutants of epidermal growth factor receptor. Crit. Rev. Oncog. 5:389-428.
    • (1994) Crit. Rev. Oncog. , vol.5 , pp. 389-428
    • Carter, T.H.1    Kung, H.J.2
  • 12
    • 0030293598 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the development of cancer
    • Coussens, L.M., and Z. Werb. 1996. Matrix metalloproteinases and the development of cancer. Chem. Biol. (Lond.) 3:895-904.
    • (1996) Chem. Biol. (Lond.) , vol.3 , pp. 895-904
    • Coussens, L.M.1    Werb, Z.2
  • 13
    • 0025887521 scopus 로고
    • Morphological characterization of cardiomyocytes isolated from a transplantable cardiac tumor derived from transgenic mouse atria (AT-1 Cells)
    • Delcarpio, J.B., N.A. Lanson, Jr., L.J. Filed, and W.C. Claycomb. 1991. Morphological characterization of cardiomyocytes isolated from a transplantable cardiac tumor derived from transgenic mouse atria (AT-1 Cells). Circ. Res. 69:1591-1600.
    • (1991) Circ. Res. , vol.69 , pp. 1591-1600
    • Delcarpio, J.B.1    Lanson Jr., N.A.2    Filed, L.J.3    Claycomb, W.C.4
  • 14
    • 0024393702 scopus 로고
    • Ligand and protein kinase C downmodulate the colony-stimulating factor 1 receptor by independent mechanisms
    • Downing, J.R., M.F. Roussel, and C.J. Sherr. 1989. Ligand and protein kinase C downmodulate the colony-stimulating factor 1 receptor by independent mechanisms. Mol. Cell. Biol. 9:2890-2896.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2890-2896
    • Downing, J.R.1    Roussel, M.F.2    Sherr, C.J.3
  • 15
    • 0029021518 scopus 로고
    • Heterodimerization and functional interaction between EGF receptor family members: A new signaling paradigm with implications for breast cancer research
    • Earp, H.S., T.L. Dawson, X. Li, and H. Yu. 1995. Heterodimerization and functional interaction between EGF receptor family members: a new signaling paradigm with implications for breast cancer research. Breast Cancer Res. Treat. 35:115-132.
    • (1995) Breast Cancer Res. Treat. , vol.35 , pp. 115-132
    • Earp, H.S.1    Dawson, T.L.2    Li, X.3    Yu, H.4
  • 16
    • 0023061283 scopus 로고
    • A membrane-anchored cytoplasmic domain of the human insulin receptor mediates a constitutively elevated insulin-independent uptake of 2-deoxyglycose
    • Ellis, L., D.O. Morgan, E. Clauser, R.A. Roth, and W.J. Rutter. 1987. A membrane-anchored cytoplasmic domain of the human insulin receptor mediates a constitutively elevated insulin-independent uptake of 2-deoxyglycose. Mol. Endocrinol. 1:15-24.
    • (1987) Mol. Endocrinol. , vol.1 , pp. 15-24
    • Ellis, L.1    Morgan, D.O.2    Clauser, E.3    Roth, R.A.4    Rutter, W.J.5
  • 17
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., R.F. Standaert, W.S. Lane, S. Choi, E.J. Corey, and S.L. Schreiber. 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science. 268:726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 18
    • 0029557613 scopus 로고
    • The epidermal growth factor receptor is covalcntly linked to ubiquitin
    • Galcheva-Oargova, Z., S.J. Therous, and R.J. Davis. 1995. The epidermal growth factor receptor is covalcntly linked to ubiquitin. Oncogene. 11:2649-2655.
    • (1995) Oncogene , vol.11 , pp. 2649-2655
    • Galcheva-Oargova, Z.1    Therous, S.J.2    Davis, R.J.3
  • 19
    • 0028785406 scopus 로고
    • Aberrant neural and cardiac development in mice lacking the ErbB4 neuregulin receptor
    • Gassmann, M., F. Casagranda, D. Orioli, H. Simon, C. Lai, R. Klein, and G. Lemke. 1995. Aberrant neural and cardiac development in mice lacking the ErbB4 neuregulin receptor. Nature (Lond.). 378:390-394.
    • (1995) Nature (Lond.) , vol.378 , pp. 390-394
    • Gassmann, M.1    Casagranda, F.2    Orioli, D.3    Simon, H.4    Lai, C.5    Klein, R.6    Lemke, G.7
  • 20
    • 0023253912 scopus 로고
    • Separate domains of the insulin receptor contain sites of autophosphorylation and tyrosine kinase activity
    • Goren, H.J., M.F. White, and C.R. Kahn. 1987. Separate domains of the insulin receptor contain sites of autophosphorylation and tyrosine kinase activity. Biochemistry. 26:2374-2382.
    • (1987) Biochemistry , vol.26 , pp. 2374-2382
    • Goren, H.J.1    White, M.F.2    Kahn, C.R.3
  • 21
    • 0029310659 scopus 로고
    • Baculovirus expression and purification of the second messenger enzyme phospholipase C-γ1, a tyrosine kinase substrate
    • Horstman, D.A., R. Ball, and G. Carpenter. 1995. Baculovirus expression and purification of the second messenger enzyme phospholipase C-γ1, a tyrosine kinase substrate. Protein Expr. Purif. 6:278-283.
    • (1995) Protein Expr. Purif. , vol.6 , pp. 278-283
    • Horstman, D.A.1    Ball, R.2    Carpenter, G.3
  • 22
    • 0024603896 scopus 로고
    • Proteolytic generation of constitutive tyrosine kinase activity of the human insulin receptor
    • Hsuan, J.J., J. Downward, S. Clark, and M.D. Waterfield. 1989. Proteolytic generation of constitutive tyrosine kinase activity of the human insulin receptor. Biochem. J. 259:519-527.
    • (1989) Biochem. J. , vol.259 , pp. 519-527
    • Hsuan, J.J.1    Downward, J.2    Clark, S.3    Waterfield, M.D.4
  • 23
    • 0031045984 scopus 로고    scopus 로고
    • Degradation of the Met tyrosine kinase receptor by the ubiquitin-proteasome pathway
    • Jeffers, M., G.A. Taylor, K.M. Weidner, S. Omura, and G.F. Vande Woude. 1997. Degradation of the Met tyrosine kinase receptor by the ubiquitin-proteasome pathway. Mol. Cell. Biol. 17:799-808.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 799-808
    • Jeffers, M.1    Taylor, G.A.2    Weidner, K.M.3    Omura, S.4    Vande Woude, G.F.5
  • 24
    • 0026576395 scopus 로고
    • Gene expression and atrial natriuretic factor processing and secretion in cultured AT-1 cardiac myocytes
    • Lanson, N.A., Jr., C.C. Glembotski, M.E. Steinhelper, L.J. Field, and W.C. Claycomb. 1992. Gene expression and atrial natriuretic factor processing and secretion in cultured AT-1 cardiac myocytes. Circulation. 85:1835-1841.
    • (1992) Circulation , vol.85 , pp. 1835-1841
    • Lanson Jr., N.A.1    Glembotski, C.C.2    Steinhelper, M.E.3    Field, L.J.4    Claycomb, W.C.5
  • 25
    • 0026098104 scopus 로고
    • Expression of inducible membrane-anchored insulin receptor kinase enhances deoxyglucose uptake
    • Lebwohl, D.E., I. Nunez, M. Chan, and O.M. Rosen. 1991. Expression of inducible membrane-anchored insulin receptor kinase enhances deoxyglucose uptake. J. Biol. Chem. 266:386-390.
    • (1991) J. Biol. Chem. , vol.266 , pp. 386-390
    • Lebwohl, D.E.1    Nunez, I.2    Chan, M.3    Rosen, O.M.4
  • 26
    • 0029812896 scopus 로고    scopus 로고
    • Ubiquitination of protein kinase C-α and degradation by the proteasome
    • Lee, H.-W., L. Smith, G.R. Pettit, A. Vinitsky, and J.B. Smith. 1996. Ubiquitination of protein kinase C-α and degradation by the proteasome. J. Biol. Chem. 271:20973-20976.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20973-20976
    • Lee, H.-W.1    Smith, L.2    Pettit, G.R.3    Vinitsky, A.4    Smith, J.B.5
  • 27
    • 0026528966 scopus 로고
    • 2-terminal truncation and fusion to avian sarcoma virus UR2 gag sequence
    • 2-terminal truncation and fusion to avian sarcoma virus UR2 gag sequence. J. Virol. 66: 374-385.
    • (1992) J. Virol. , vol.66 , pp. 374-385
    • Liu, D.1    Rutter, W.J.2    Wang, L.-H.3
  • 28
    • 0027402605 scopus 로고
    • Modulating effects of the extracellular sequence of the human insulinlike growth factor I receptor on its transforming and tumorigenic potential
    • Liu, D., W.J. Rutter, and L.-H. Wang. 1993. Modulating effects of the extracellular sequence of the human insulinlike growth factor I receptor on its transforming and tumorigenic potential. J. Virol. 67:9-18.
    • (1993) J. Virol. , vol.67 , pp. 9-18
    • Liu, D.1    Rutter, W.J.2    Wang, L.-H.3
  • 29
    • 0026336188 scopus 로고
    • Enhanced tumorigenesis of NR6 cells which express nondownregulating epidermal growth factor receptors
    • Masui, H., A. Wells, C.S. Lazar, M.G. Rosenfeld, and G. Gill. 1991. Enhanced tumorigenesis of NR6 cells which express nondownregulating epidermal growth factor receptors. Cancer Res. 51:6170-6175.
    • (1991) Cancer Res. , vol.51 , pp. 6170-6175
    • Masui, H.1    Wells, A.2    Lazar, C.S.3    Rosenfeld, M.G.4    Gill, G.5
  • 30
    • 0029812759 scopus 로고    scopus 로고
    • c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
    • c-erbB-2 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
  • 31
    • 0028158499 scopus 로고
    • Ligand-dependent polyubiquitination of c-kit gene product:a possible mechanism of receptor down modulation in M07e cells
    • Miyazawa, K., K. Toyama, A. Gotoh, P.C. Hendrie, C. Mantel, and H.E. Broxmeyer. 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
  • 33
    • 0026664626 scopus 로고
    • Ligand-induced polyubiquitination of the platelet-derived growth factor β-receptor
    • Mori, S., C.-H. Heldin, and L. Claesson-Welsh. 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
  • 35
    • 0028938732 scopus 로고
    • The transforming receptor tyrosine kinase, Axl, is posttranslationally regulated by proteolytic cleavage
    • O'Bryan, J.P., Y.-W. Fridell, R. Koski, B. Varnum, and E.T. Liu. 1995. The transforming receptor tyrosine kinase, Axl, is posttranslationally regulated by proteolytic cleavage. J. Biol. Chem. 270:551-557.
    • (1995) J. Biol. Chem. , vol.270 , pp. 551-557
    • O'Bryan, J.P.1    Fridell, Y.-W.2    Koski, R.3    Varnum, B.4    Liu, E.T.5
  • 39
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K.L., C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, and A.L. Goldberg. 1994. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell. 78:761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 40
    • 0015502199 scopus 로고
    • Epidermal growth factor and a new derivative. Rapid isolation procedures and biological and chemical characterization
    • Savage, C.R., and S. Cohen. 1972. Epidermal growth factor and a new derivative. Rapid isolation procedures and biological and chemical characterization. J. Biol. Chem. 247:7609-7611.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7609-7611
    • Savage, C.R.1    Cohen, S.2
  • 41
    • 0023913099 scopus 로고
    • Tryptic activation of the insulin receptor. Proteolytic truncation of the α-subunit releases the β-subunit from inhibitory control
    • Shoelson, S.E., M.F. White, and C.R. Kahn. 1988. Tryptic activation of the insulin receptor. Proteolytic truncation of the α-subunit releases the β-subunit from inhibitory control. J. Biol. Chem. 263:4852-4860.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4852-4860
    • Shoelson, S.E.1    White, M.F.2    Kahn, C.R.3
  • 43
    • 0027620152 scopus 로고
    • Endocytosis of growth factor receptors
    • Sorkin, A., and C.M. Waters. 1993. Endocytosis of growth factor receptors. BioEssays. 6:375-382.
    • (1993) BioEssays , vol.6 , pp. 375-382
    • Sorkin, A.1    Waters, C.M.2
  • 45
    • 0027971393 scopus 로고
    • ErbB-3 and ErbB-4 function as the respective low and high affinity receptors of all Neu differentiation factor/heregulin isoforms
    • Tzahar, E., G. Levkowitz, D. Karunagaran, L. Yi, E. Peles, S. Lavi, D. Chang, N. Liu, A. Yayon, D. Wen, and Y. Yarden. 1994. ErbB-3 and ErbB-4 function as the respective low and high affinity receptors of all Neu differentiation factor/heregulin isoforms. J. Biol. Chem. 269:25226-25233.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25226-25233
    • Tzahar, E.1    Levkowitz, G.2    Karunagaran, D.3    Yi, L.4    Peles, E.5    Lavi, S.6    Chang, D.7    Liu, N.8    Yayon, A.9    Wen, D.10    Yarden, Y.11
  • 46
    • 0029764504 scopus 로고    scopus 로고
    • Selective cleavage of the heregulin receptor ErbB-4 by protein kinase C activation
    • Vecchi, M., J. Baulida, and G. Carpenter. 1996. Selective cleavage of the heregulin receptor ErbB-4 by protein kinase C activation. J. Biol. Chem. 271: 18989-18995.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18989-18995
    • Vecchi, M.1    Baulida, J.2    Carpenter, G.3
  • 48
    • 0025139326 scopus 로고
    • Ligand-induced transformation by noninternalizing epidermal growth factor receptor
    • Wells, A., J.B. Welsh, C.S. Lazar, H.S. Wiley, G.N. Gill, and M.G. Rosenfeld. 1990. Ligand-induced transformation by noninternalizing epidermal growth factor receptor. Science. 247:962-964.
    • (1990) Science , vol.247 , pp. 962-964
    • Wells, A.1    Welsh, J.B.2    Lazar, C.S.3    Wiley, H.S.4    Gill, G.N.5    Rosenfeld, M.G.6
  • 49
    • 0029739346 scopus 로고    scopus 로고
    • Regulation of sodium current development in cultured atrial tumor myocytes (AT-1 cells)
    • Yang, T., and D.M. Roden. 1996. Regulation of sodium current development in cultured atrial tumor myocytes (AT-1 cells). Am. J. Physiol. 271:H541-H547.
    • (1996) Am. J. Physiol. , vol.271
    • Yang, T.1    Roden, D.M.2
  • 52
    • 0027157536 scopus 로고
    • Mechanism of kit ligand, phorbol ester, and calcium-induced down regulation of c-kit receptors in mast cells
    • Yee, N.S., H. Langen, and P. Besmer. 1993. Mechanism of kit ligand, phorbol ester, and calcium-induced down regulation of c-kit receptors in mast cells. J. Biol. Chem. 268:14189-14201.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14189-14201
    • Yee, N.S.1    Langen, H.2    Besmer, P.3


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