메뉴 건너뛰기




Volumn 8, Issue 11, 1997, Pages 2133-2143

Distinct endocytic responses of heteromeric and homomeric transforming growth factor β receptors

Author keywords

[No Author keywords available]

Indexed keywords

GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; LIGAND; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR;

EID: 0030728295     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.8.11.2133     Document Type: Article
Times cited : (56)

References (61)
  • 1
    • 0029832696 scopus 로고    scopus 로고
    • Chimeric granulocyte/macrophage colony-stimulating factor/transforming growth factor-β (TGF-β) receptors define a model system for investigating the role of homomeric and heteromeric receptors in TGF-β signaling
    • Anders, R.A., and Leof, E.B. (1996). Chimeric granulocyte/macrophage colony-stimulating factor/transforming growth factor-β (TGF-β) receptors define a model system for investigating the role of homomeric and heteromeric receptors in TGF-β signaling. J. Biol. Chem. 271, 21758-21766.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21758-21766
    • Anders, R.A.1    Leof, E.B.2
  • 2
    • 0029912203 scopus 로고    scopus 로고
    • All ErbB receptors other than the epidermal growth factor receptors are endocytosis impaired
    • Baulida, J., Kraus, M.H., Maurizio, A., Di Fiore, P.P. and Carpenter, G. (1996). All ErbB receptors other than the epidermal growth factor receptors 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    Maurizio, A.3    Di Fiore, P.P.4    Carpenter, G.5
  • 3
    • 0027203952 scopus 로고
    • Ligand-induced internalization of the epidermal growth factor receptor is mediated by multiple endocytic codes analogous to the tyrosine motif found in constitutively internalized receptors
    • Chang, C.P. et al. (1993). Ligand-induced internalization of the epidermal growth factor receptor is mediated by multiple endocytic codes analogous to the tyrosine motif found in constitutively internalized receptors. J. Biol. Chem. 268, 19312-19320.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19312-19320
    • Chang, C.P.1
  • 4
    • 0028059199 scopus 로고
    • Homomeric interactions between type II transforming growth factor-beta receptors
    • Chen, R.H., and Derynck, R. (1994). Homomeric interactions between type II transforming growth factor-beta receptors. J. Biol. Chem. 269, 22868-22874.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22868-22874
    • Chen, R.H.1    Derynck, R.2
  • 5
    • 0028138642 scopus 로고
    • Clathrin polymerization is not required for bulk-phase endocytosis in rat fetal fibroblasts
    • Cupers, P., Veithen, A., Kiss, A., Baudhuin, P., and Courtoy, P.J. (1994). Clathrin polymerization is not required for bulk-phase endocytosis in rat fetal fibroblasts. J. Cell Biol. 127, 725-735.
    • (1994) J. Cell Biol. , vol.127 , pp. 725-735
    • Cupers, P.1    Veithen, A.2    Kiss, A.3    Baudhuin, P.4    Courtoy, P.J.5
  • 6
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic coated vesicle formation
    • Damke, H., Baba, T., Warnock, D.E. and Schmid, S.L. (1994). Induction of mutant dynamin specifically blocks endocytic coated vesicle formation. J. Cell Biol. 127, 915-934.
    • (1994) J. Cell Biol. , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 7
    • 0029064474 scopus 로고
    • Specific binding of endocrine transforming growth factor-beta 1 to vascular endothelium
    • Dickson, K., Philip, A., Warshawsky, H., O'Connor-McCourt, M., and Bergeron, J.J. (1995). Specific binding of endocrine transforming growth factor-beta 1 to vascular endothelium. J. Clin. Invest. 95, 2539-2554.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2539-2554
    • Dickson, K.1    Philip, A.2    Warshawsky, H.3    O'Connor-McCourt, M.4    Bergeron, J.J.5
  • 8
    • 0029097308 scopus 로고
    • Dynamic or stable interactions of influenza hemagglutinin mutants with coated pits: Dependence on the internalization signal but not on aggregation
    • Fire, E., Gutman, O., Roth, M.G., and Henis, Y.I. (1995). Dynamic or stable interactions of influenza hemagglutinin mutants with coated pits: dependence on the internalization signal but not on aggregation. J. Biol. Chem. 270, 21075-21081.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21075-21081
    • Fire, E.1    Gutman, O.2    Roth, M.G.3    Henis, Y.I.4
  • 9
    • 0021202508 scopus 로고
    • Characterization of a membrane receptor for transforming growth factor-β in normal rat kidney fibroblasts
    • Frolik, C.A., Wakefield, L.M., Smith, D.M., and Sporn, M.B. (1984). Characterization of a membrane receptor for transforming growth factor-β in normal rat kidney fibroblasts. J. Biol. Chem. 259, 10995-11000.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10995-11000
    • Frolik, C.A.1    Wakefield, L.M.2    Smith, D.M.3    Sporn, M.B.4
  • 10
    • 0029989302 scopus 로고    scopus 로고
    • Growth hormone (GH) and a GH antagonist promote GH receptor dimerization and internalization
    • Harding, P.A., Wang, X., Okada, S., Chen, W.Y., Wan, W., and Kopchick, J.J. (1996). Growth hormone (GH) and a GH antagonist promote GH receptor dimerization and internalization. J. Biol. Chem. 271, 6708-6712.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6708-6712
    • Harding, P.A.1    Wang, X.2    Okada, S.3    Chen, W.Y.4    Wan, W.5    Kopchick, J.J.6
  • 11
    • 0025637605 scopus 로고
    • Molecular cloning of a second subunit of the receptor for human granulocyte-macrophage colony-stimulating factor (GM-CSF): Reconstitution of a high-affinity GM-CSF receptor
    • Hayashida, K., Kitamura, T., Gorman, D.M., Arai, K.-I., Yokota, T., and Miyajima, A. (1990). Molecular cloning of a second subunit of the receptor for human granulocyte-macrophage colony-stimulating factor (GM-CSF): reconstitution of a high-affinity GM-CSF receptor. Proc. Natl. Acad. Sci. USA 87, 9655-9659.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9655-9659
    • Hayashida, K.1    Kitamura, T.2    Gorman, D.M.3    Arai, K.I.4    Yokota, T.5    Miyajima, A.6
  • 12
    • 0028291369 scopus 로고
    • The types II and III transforming growth factor-beta receptors form homo-oligomers
    • Henis, Y.I., Moustakas, A., Lin, H.Y., and Lodish, H.F. (1994). The types II and III transforming growth factor-beta receptors form homo-oligomers. J. Cell Biol. 126, 139-154.
    • (1994) J. Cell Biol. , vol.126 , pp. 139-154
    • Henis, Y.I.1    Moustakas, A.2    Lin, H.Y.3    Lodish, H.F.4
  • 13
    • 0028211773 scopus 로고
    • The coated pit and macropinocytic pathways serve distinct endosome populations
    • Hewlett, L.J., Prescott, A.R., and Watts, C. (1994). The coated pit and macropinocytic pathways serve distinct endosome populations. J. Cell Biol. 124, 689-703.
    • (1994) J. Cell Biol. , vol.124 , pp. 689-703
    • Hewlett, L.J.1    Prescott, A.R.2    Watts, C.3
  • 14
    • 0028180315 scopus 로고
    • The TGF beta superfamily: New member, new receptors, and new genetic tests of function in different organisms
    • Kingsley, D.M. (1994). The TGF beta superfamily: new member, new receptors, and new genetic tests of function in different organisms. Genes Dev. 8, 133-146.
    • (1994) Genes Dev. , vol.8 , pp. 133-146
    • Kingsley, D.M.1
  • 15
    • 0025861759 scopus 로고
    • Expression cloning of the human IL-3 receptor cDNA reveals a shared beta subunit for the human IL-3 and GM-CSF receptors
    • Kitamura, T., Sato, N., Arai, K., and Miyajima, A. (1991). Expression cloning of the human IL-3 receptor cDNA reveals a shared beta subunit for the human IL-3 and GM-CSF receptors. Cell 66, 1165-1174.
    • (1991) Cell , vol.66 , pp. 1165-1174
    • Kitamura, T.1    Sato, N.2    Arai, K.3    Miyajima, A.4
  • 16
    • 0030965611 scopus 로고    scopus 로고
    • Processing of the transforming growth factor β type I and type II receptors
    • Koli, K.M., and Arleaga, C.L. (1997). Processing of the transforming growth factor β type I and type II receptors. J. Biol. Chem. 272, 6423-6427.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6423-6427
    • Koli, K.M.1    Arleaga, C.L.2
  • 17
    • 0029834067 scopus 로고    scopus 로고
    • Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways
    • Lagna, G., Hata, A., Hemmati-Brivanlou, A., and Massagué, J. (1996). Partnership between DPC4 and SMAD proteins in TGF-β signalling pathways. Nature 383, 832-836.
    • (1996) Nature , vol.383 , pp. 832-836
    • Lagna, G.1    Hata, A.2    Hemmati-Brivanlou, A.3    Massagué, J.4
  • 18
    • 0029117498 scopus 로고
    • The emergence of clathrin-independent pinocytic pathways
    • Lamaze, C., and Schmid, S. (1995). The emergence of clathrin-independent pinocytic pathways. Curr. Opin. Cell Biol. 7, 573-580.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 573-580
    • Lamaze, C.1    Schmid, S.2
  • 19
    • 0020626609 scopus 로고
    • Depletion of intracellular potassium arrests coated pit formation and receptor mediated endocytosis in fibroblasts
    • Larkin, J.M., Brown, M.S., Goldstein, J.L., and Anderson, R.G.W. (1983). Depletion of intracellular potassium arrests coated pit formation and receptor mediated endocytosis in fibroblasts. Cell 33, 273-285.
    • (1983) Cell , vol.33 , pp. 273-285
    • Larkin, J.M.1    Brown, M.S.2    Goldstein, J.L.3    Anderson, R.G.W.4
  • 20
    • 0030013242 scopus 로고    scopus 로고
    • Serine phosphorylation, chromosomal localization, and transforming growth factor-β signal transduction by human bsp-1
    • Lechleider, R.J., de Caesteckert, M.P., Dehejia, A., Polymeropoulos, M.H., and Roberts, A.B. (1996). Serine phosphorylation, chromosomal localization, and transforming growth factor-β signal transduction by human bsp-1. J. Biol. Chem. 271, 17617-17620.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17617-17620
    • Lechleider, R.J.1    De Caesteckert, M.P.2    Dehejia, A.3    Polymeropoulos, M.H.4    Roberts, A.B.5
  • 21
    • 0029792338 scopus 로고    scopus 로고
    • Signaling by chimeric erythropoietin-TGFβ receptors: Homodimerization of the cytoplasmic domain of the type I TGFβ receptor and heterodimerization iwth the type II receptor are both required for intracellular signal transduction
    • Luo, K., and Lodish, H.F. (1996). Signaling by chimeric erythropoietin-TGFβ receptors: homodimerization of the cytoplasmic domain of the type I TGFβ receptor and heterodimerization iwth the type II receptor are both required for intracellular signal transduction. EMBO J. 15, 4485-4496.
    • (1996) EMBO J. , vol.15 , pp. 4485-4496
    • Luo, K.1    Lodish, H.F.2
  • 22
    • 0030300115 scopus 로고    scopus 로고
    • MADR2 is a substrate of the TGFβ receptor and its phosphorylation is required for nuclear accumulation and signaling
    • Macias-Silva, M., Abdollah, S., Hoodless, P., Pirone, R., Attisano, L., and Wrana, J.L. (1996). MADR2 is a substrate of the TGFβ receptor and its phosphorylation is required for nuclear accumulation and signaling. Cell 87, 1215-1224.
    • (1996) Cell , vol.87 , pp. 1215-1224
    • Macias-Silva, M.1    Abdollah, S.2    Hoodless, P.3    Pirone, R.4    Attisano, L.5    Wrana, J.L.6
  • 23
    • 0030199031 scopus 로고    scopus 로고
    • Bacterial superantigens induce V beta-specific T cell receptor internalization
    • Makida, R., Hofer, M.F., Takase, K., Cambier, J.C., and Leung, D.Y. (1996). Bacterial superantigens induce V beta-specific T cell receptor internalization. Mol. Immunol. 33, 891-900.
    • (1996) Mol. Immunol. , vol.33 , pp. 891-900
    • Makida, R.1    Hofer, M.F.2    Takase, K.3    Cambier, J.C.4    Leung, D.Y.5
  • 24
    • 0023245751 scopus 로고
    • Rapid analytical and preparative isolation of functional endosomes by free flow electrophoresis
    • Marsh, M., Schmid, S., Kern, H., Harms, E., Male, P., Mellman, I., and Helenius, A. (1987). Rapid analytical and preparative isolation of functional endosomes by free flow electrophoresis. J. Cell Biol. 104, 875-886.
    • (1987) J. Cell Biol. , vol.104 , pp. 875-886
    • Marsh, M.1    Schmid, S.2    Kern, H.3    Harms, E.4    Male, P.5    Mellman, I.6    Helenius, A.7
  • 25
    • 0006551294 scopus 로고
    • Type-β transforming growth factor receptors in cells chronically exposed to the Hgand
    • Massagué, J. (1985). Type-β transforming growth factor receptors in cells chronically exposed to the Hgand. Cancer Cells 3, 73-78.
    • (1985) Cancer Cells , vol.3 , pp. 73-78
    • Massagué, J.1
  • 26
    • 0030604542 scopus 로고    scopus 로고
    • TGFβ signaling: Receptors, transducers, and mad proteins
    • Massagué, J. (1996). TGFβ signaling: receptors, transducers, and mad proteins. Cell 85, 947-950.
    • (1996) Cell , vol.85 , pp. 947-950
    • Massagué, J.1
  • 28
    • 0025122809 scopus 로고
    • TGF-β receptors and TGF-β binding proteoglycans: Recent progress in identifying their functional properties
    • Massagué, J., Cheifetz, S., Boyd, F.T., and Andres, J.L. (1990). TGF-β receptors and TGF-β binding proteoglycans: recent progress in identifying their functional properties. Ann. N.Y. Acad. Sci. 593, 59-72.
    • (1990) Ann. N.Y. Acad. Sci. , vol.593 , pp. 59-72
    • Massagué, J.1    Cheifetz, S.2    Boyd, F.T.3    Andres, J.L.4
  • 29
    • 0022549763 scopus 로고
    • Internalization of transforming growth factor-β and its receptor in BALB/c 3T3 fibroblasts
    • Massagué, J., and Kelly, B. (1986). Internalization of transforming growth factor-β and its receptor in BALB/c 3T3 fibroblasts. J. Cell. Physiol. 128, 216-222.
    • (1986) J. Cell. Physiol. , vol.128 , pp. 216-222
    • Massagué, J.1    Kelly, B.2
  • 30
    • 0021992459 scopus 로고
    • Cellular receptors for type β transforming growth factor
    • Massagué, J., and Like, B. (1985). Cellular receptors for type β transforming growth factor. J. Biol. Chem. 260, 2636-2645.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2636-2645
    • Massagué, J.1    Like, B.2
  • 31
    • 0030899939 scopus 로고    scopus 로고
    • A chimeric serine/threonine kinase receptor system reveals the potential of multiple type II receptors to cooperate with transforming growth factor-β
    • Muramatsu, M., Yan, J., Eto, K., Tomoda, T., Yamada, R., and Arai, K. (1997). A chimeric serine/threonine kinase receptor system reveals the potential of multiple type II receptors to cooperate with transforming growth factor-β. Mol. Biol. Cell 8, 469-480.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 469-480
    • Muramatsu, M.1    Yan, J.2    Eto, K.3    Tomoda, T.4    Yamada, R.5    Arai, K.6
  • 32
    • 0031034589 scopus 로고    scopus 로고
    • Identification of Smad2, a human Mad-related protein in the transforming growth factor β signaling pathway
    • Nakao, A., Roijer, E., Imamura, T., Souchelnytskyi, S., Stenman, G., Heldin, C.-H., and ten Dijke, P. (1997). Identification of Smad2, a human Mad-related protein in the transforming growth factor β signaling pathway. J. Biol. Chem. 272, 2896-2900.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2896-2900
    • Nakao, A.1    Roijer, E.2    Imamura, T.3    Souchelnytskyi, S.4    Stenman, G.5    Heldin, C.-H.6    Ten Dijke, P.7
  • 33
    • 0029037863 scopus 로고
    • Ligand-induced endocytosis of epidermal growth factor receptors that are defective in binding adaptor proteins
    • Nesterov, A., Wiley, H.S., and Gill, G.N. (1995). Ligand-induced endocytosis of epidermal growth factor receptors that are defective in binding adaptor proteins. Proc. Natl. Acad. Sci. USA 92, 8719-8723.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8719-8723
    • Nesterov, A.1    Wiley, H.S.2    Gill, G.N.3
  • 34
    • 0025887628 scopus 로고
    • Purification of a new type high molecular weight receptor (type V receptor) of transforming growth factor beta (TGF-beta) from bovine liver. Identification of the type V TGF-beta receptor in cultured cells
    • O'Grady, P., Kuo, M.D., Baldassare, J. J., Huang, S.S., and Huang, J.S. (1991). Purification of a new type high molecular weight receptor (type V receptor) of transforming growth factor beta (TGF-beta) from bovine liver. Identification of the type V TGF-beta receptor in cultured cells. J. Biol. Chem. 266, 8583-8589.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8583-8589
    • O'Grady, P.1    Kuo, M.D.2    Baldassare, J.J.3    Huang, S.S.4    Huang, J.S.5
  • 35
    • 0025038705 scopus 로고
    • Functional reconstitution of the human epidermal growth factor receptor system in Xenopus oocytes
    • Opresko, L.K., and Wiley, H.S. (1990). Functional reconstitution of the human epidermal growth factor receptor system in Xenopus oocytes. J. Cell Biol. 111, 1661-1671.
    • (1990) J. Cell Biol. , vol.111 , pp. 1661-1671
    • Opresko, L.K.1    Wiley, H.S.2
  • 37
    • 0029077554 scopus 로고
    • Chimeric receptors expressing juxtamembrane sequences of the insulin receptor undergo rapid endocytosis in the absence of receptor tyrosine kinase activity
    • Rajagopalan, M., Hebert, L., and McClain, D.A. (1995). Chimeric receptors expressing juxtamembrane sequences of the insulin receptor undergo rapid endocytosis in the absence of receptor tyrosine kinase activity. Biochem. Biophys. Res. Commun. 211, 714-718.
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 714-718
    • Rajagopalan, M.1    Hebert, L.2    McClain, D.A.3
  • 38
    • 0026356392 scopus 로고
    • Amino acid sequences Gly-Pro-Leu-Tyr and Asn-Pro-Glu-Tyr in the sub-membranous domain of the insulin receptor are required for normal endocytosis
    • Rajagopalan, M., Neidigh, J.L., and McClain, D.A. (1991). Amino acid sequences Gly-Pro-Leu-Tyr and Asn-Pro-Glu-Tyr in the sub-membranous domain of the insulin receptor are required for normal endocytosis. J. Biol. Chem. 266, 23068-23073.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23068-23073
    • Rajagopalan, M.1    Neidigh, J.L.2    McClain, D.A.3
  • 39
    • 0028038006 scopus 로고
    • Growth factor-mediated mechanisms of nicotine-dependent carcinogenesis
    • Rakowicz-Szulczynska, E.M., McIntosh, D.G., and Smith, M. (1994). Growth factor-mediated mechanisms of nicotine-dependent carcinogenesis. Carcinogenesis 15, 1839-1846.
    • (1994) Carcinogenesis , vol.15 , pp. 1839-1846
    • Rakowicz-Szulczynska, E.M.1    McIntosh, D.G.2    Smith, M.3
  • 40
    • 0021343874 scopus 로고
    • Down-regulation of gonadotropin receptors in a murine Leydig tumor cell line
    • Rebois, R.V., and Fishman, P.H. (1984). Down-regulation of gonadotropin receptors in a murine Leydig tumor cell line. J. Biol. Chem. 259, 3096-3101.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3096-3101
    • Rebois, R.V.1    Fishman, P.H.2
  • 41
    • 0025781047 scopus 로고
    • Binding and internalization of transforming growth factor-β1 by human hepatoma cells: Evidence for receptor recycling
    • Sathre, K.A., Tsang, M.L.-S., Weatherbee, J.A., and Steer, C.J. (1991). Binding and internalization of transforming growth factor-β1 by human hepatoma cells: evidence for receptor recycling. Hepatology 14, 287-295.
    • (1991) Hepatology , vol.14 , pp. 287-295
    • Sathre, K.A.1    Tsang, M.L.S.2    Weatherbee, J.A.3    Steer, C.J.4
  • 42
    • 0026928718 scopus 로고
    • The mechanism of receptor-mediated endocytosis: More questions than answers
    • Schmid, S.L. (1992). The mechanism of receptor-mediated endocytosis: more questions than answers. BioEssays 14, 589-596.
    • (1992) BioEssays , vol.14 , pp. 589-596
    • Schmid, S.L.1
  • 43
    • 0025986011 scopus 로고
    • The amino-terminal helix of GM-CSF and IL-5 governs high affinity binding to their receptors
    • Shanafelt, A.B., Miyajima, A., Kitamura, T., and Kastelein, R.A. (1991). The amino-terminal helix of GM-CSF and IL-5 governs high affinity binding to their receptors. EMBO J. 10, 4105-4112.
    • (1991) EMBO J. , vol.10 , pp. 4105-4112
    • Shanafelt, A.B.1    Miyajima, A.2    Kitamura, T.3    Kastelein, R.A.4
  • 44
    • 0029889579 scopus 로고    scopus 로고
    • Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr-974-containing internalization motif
    • Sorkin, A., Mazzotti, M., Sorkin, T., Scotto, L., and Beguinot, L. (1996). Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr-974-containing internalization motif. J. Biol. Chem. 271, 13377-13384.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13377-13384
    • Sorkin, A.1    Mazzotti, M.2    Sorkin, T.3    Scotto, L.4    Beguinot, L.5
  • 45
    • 0028944988 scopus 로고
    • Stoichiometric interaction of the epidermal growth factor receptor with the clathrin-associated protein complex AP-2
    • Sorkin, A., McKinsey, T., Shih, W., Kirchhausen, T., and Carpenter, G. (1995). Stoichiometric interaction of the epidermal growth factor receptor with the clathrin-associated protein complex AP-2. J. Biol. Chem. 270, 619-625.
    • (1995) J. Biol. Chem. , vol.270 , pp. 619-625
    • Sorkin, A.1    McKinsey, T.2    Shih, W.3    Kirchhausen, T.4    Carpenter, G.5
  • 46
    • 0027620152 scopus 로고
    • Endocytosis of growth factor receptors
    • Sorkin, A., and Water, C.M. (1993). Endocytosis of growth factor receptors. BioEssays 15, 375-382.
    • (1993) BioEssays , vol.15 , pp. 375-382
    • Sorkin, A.1    Water, C.M.2
  • 48
    • 0027333415 scopus 로고
    • Signal-dependent membrane protein trafficking in the endocytic pathway
    • Trowbridge, I.S., Collawn, J.F., and Hopkins, C.R. (1993). Signal-dependent membrane protein trafficking in the endocytic pathway. Annu. Rev. Cell Biol. 9, 129-161.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 129-161
    • Trowbridge, I.S.1    Collawn, J.F.2    Hopkins, C.R.3
  • 49
    • 0029163614 scopus 로고
    • Carboxy-terminal domains determine internalization and recyling characteristics of bombesin receptor chimeras
    • Tseng, M., Detjen, K., Struck, V., and Logsdon, C.D. (1995). Carboxy-terminal domains determine internalization and recyling characteristics of bombesin receptor chimeras. J. Biol. Chem. 270, 18858-18864.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18858-18864
    • Tseng, M.1    Detjen, K.2    Struck, V.3    Logsdon, C.D.4
  • 50
    • 0031026631 scopus 로고    scopus 로고
    • The dynamins: Redundant or distinct functions for an expanding family of related GTPases
    • Urrutia, R., Henley, J.R., Cook, T., and McNiven, M.A. (1997). The dynamins: redundant or distinct functions for an expanding family of related GTPases. Proc. Natl. Acad. Sci. USA 94, 377-384.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 377-384
    • Urrutia, R.1    Henley, J.R.2    Cook, T.3    McNiven, M.A.4
  • 51
    • 0023604578 scopus 로고
    • Distribution and modulation of the cellular receptor for transforming growth factor-β
    • Wakefield, L.M., Smith, D.M., Masui, T., Harris, C.C., and Sporn, M.B. (1987). Distribution and modulation of the cellular receptor for transforming growth factor-β. J. Cell Biol. 105, 965-975.
    • (1987) J. Cell Biol. , vol.105 , pp. 965-975
    • Wakefield, L.M.1    Smith, D.M.2    Masui, T.3    Harris, C.C.4    Sporn, M.B.5
  • 52
    • 0027409373 scopus 로고
    • Reconstituted human granulocyte-macrophage colony-stimulating factor receptor transduces growth-promoting signals in mouse NIH 3T3 cells: Comparison with signalling in BA/F3 pro-B cells
    • Watanabe, S., Mui, A.L.-F., Muto, A., Chen, J.X., Hayashida, K., Yokota, T., Miyajima, A., and Arai, K. (1993). Reconstituted human granulocyte-macrophage colony-stimulating factor receptor transduces growth-promoting signals in mouse NIH 3T3 cells: comparison with signalling in BA/F3 pro-B cells. Mol. Cell. Biol. 13, 1440-1448.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1440-1448
    • Watanabe, S.1    Mui, A.L.F.2    Muto, A.3    Chen, J.X.4    Hayashida, K.5    Yokota, T.6    Miyajima, A.7    Arai, K.8
  • 53
    • 0025240654 scopus 로고
    • Rate constants for binding, dissociation, and internalization of EGF: Effect of receptor occupancy and ligand concentration
    • Waters, C.M., Oberg, K.C., Carpenter, G., and Overholser, K.A. (1990). Rate constants for binding, dissociation, and internalization of EGF: effect of receptor occupancy and ligand concentration. Biochemistry 29, 3563-3569.
    • (1990) Biochemistry , vol.29 , pp. 3563-3569
    • Waters, C.M.1    Oberg, K.C.2    Carpenter, G.3    Overholser, K.A.4
  • 54
    • 0030030373 scopus 로고    scopus 로고
    • Complementation between kinase-defective and activation-defective TGF-beta receptors reveals a novel form of receptor cooperativity essential for signaling
    • Weis-Garcia, F., and Massagué, J. (1996). Complementation between kinase-defective and activation-defective TGF-beta receptors reveals a novel form of receptor cooperativity essential for signaling. EMBO J. 15, 276-289.
    • (1996) EMBO J. , vol.15 , pp. 276-289
    • Weis-Garcia, F.1    Massagué, J.2
  • 55
    • 0024836461 scopus 로고
    • Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells
    • West, M.A., Bretscher, M.S., and Watts, C. (1989). Distinct endocytotic pathways in epidermal growth factor-stimulated human carcinoma A431 cells. J. Cell Biol. 109, 2731-2739.
    • (1989) J. Cell Biol. , vol.109 , pp. 2731-2739
    • West, M.A.1    Bretscher, M.S.2    Watts, C.3
  • 56
    • 0019945866 scopus 로고
    • The endocytotic rate constant.A cellular parameter for quantitating receptor-mediated endocytosis
    • Wiley, H.S., and Cunningham, D.D. (1982). The endocytotic rate constant.A cellular parameter for quantitating receptor-mediated endocytosis. J. Biol. Chem. 257, 4222-4229.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4222-4229
    • Wiley, H.S.1    Cunningham, D.D.2
  • 59
    • 0027930903 scopus 로고
    • Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-beta
    • Yamashita, H., ten Dijke, P., Franzen, P., Miyazono, K., and Heldin, C.H. (1994). Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-beta. J. Biol. Chem. 269, 20172-20178.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20172-20178
    • Yamashita, H.1    Ten Dijke, P.2    Franzen, P.3    Miyazono, K.4    Heldin, C.H.5
  • 60
    • 0029833909 scopus 로고    scopus 로고
    • Mammalian dwarfins are phosphorylated in response to transforming growth factor β and are implicated in control of cell growth
    • Yingling, J.M., Das, P., Savage, C., Zhang, M., Radgett, R.W., and Wang, X.-F. (1996). Mammalian dwarfins are phosphorylated in response to transforming growth factor β and are implicated in control of cell growth. Proc. Natl. Acad. SCi. USA 93, 8940-8944.
    • (1996) Proc. Natl. Acad. SCi. USA , vol.93 , pp. 8940-8944
    • Yingling, J.M.1    Das, P.2    Savage, C.3    Zhang, M.4    Radgett, R.W.5    Wang, X.F.6
  • 61
    • 0028856547 scopus 로고
    • Regulation of transforming growth factor beta receptors in H-ras oncogene-transformed rat epithelial cells
    • Zhao, J., and Buick, R.N. (1995). Regulation of transforming growth factor beta receptors in H-ras oncogene-transformed rat epithelial cells. Cancer Res. 55, 6181-6188.
    • (1995) Cancer Res. , vol.55 , pp. 6181-6188
    • Zhao, J.1    Buick, R.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.