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Volumn 5, Issue 215, 2012, Pages

Regulation of the EGF transcriptional response by endocytic sorting

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; ESCRT PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR YY1; EGFR PROTEIN, HUMAN;

EID: 84858174818     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2002351     Document Type: Article
Times cited : (70)

References (84)
  • 2
    • 0022639836 scopus 로고
    • Receptor-mediated endocytosis of epidermal growth factor by rat hepatocytes: Receptor pathway
    • W. A. Dunn, T. P. Connolly, A. L. Hubbard, Receptor-mediated endocytosis of epidermal growth factor by rat hepatocytes: Receptor pathway. J. Cell Biol. 102, 24-36 (1986).
    • (1986) J. Cell Biol. , vol.102 , pp. 24-36
    • Dunn, W.A.1    Connolly, T.P.2    Hubbard, A.L.3
  • 3
    • 0022602283 scopus 로고
    • Localization of the epidermal growth factor (EGF) receptor within the endosome of EGF-stimulated epidermoid carcinoma (A431) cells
    • K. Miller, J. Beardmore, H. Kanety, J. Schlessinger, C. R. Hopkins, Localization of the epidermal growth factor (EGF) receptor within the endosome of EGF-stimulated epidermoid carcinoma (A431) cells. J. Cell Biol. 102, 500-509 (1986).
    • (1986) J. Cell Biol. , vol.102 , pp. 500-509
    • Miller, K.1    Beardmore, J.2    Kanety, H.3    Schlessinger, J.4    Hopkins, C.R.5
  • 4
    • 0022635389 scopus 로고
    • Binding and internalization of epidermal growth factor in human term placental cells in culture
    • W. H. Lai, H. J. Guyda, J. J. Bergeron, Binding and internalization of epidermal growth factor in human term placental cells in culture. Endocrinology 118, 413-423 (1986).
    • (1986) Endocrinology , vol.118 , pp. 413-423
    • Lai, W.H.1    Guyda, H.J.2    Bergeron, J.J.3
  • 5
    • 47149092772 scopus 로고    scopus 로고
    • Multivesicular bodies: Co-ordinated progression to maturity
    • P. G. Woodman, C. E. Futter, Multivesicular bodies: Co-ordinated progression to maturity. Curr. Opin. Cell Biol. 20, 408-414 (2008).
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 408-414
    • Woodman, P.G.1    Futter, C.E.2
  • 6
    • 37749018903 scopus 로고    scopus 로고
    • Biogenesis and function of multivesicular bodies
    • R. C. Piper, D. J. Katzmann, Biogenesis and function of multivesicular bodies. Annu. Rev. Cell Dev. Biol. 23, 519-547 (2007).
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 519-547
    • Piper, R.C.1    Katzmann, D.J.2
  • 7
    • 77954957013 scopus 로고    scopus 로고
    • Membrane budding and scission by the ESCRT machinery: It's all in the neck
    • J. H. Hurley, P. I. Hanson, Membrane budding and scission by the ESCRT machinery: It's all in the neck. Nat. Rev. Mol. Cell Biol. 11, 556-566 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 556-566
    • Hurley, J.H.1    Hanson, P.I.2
  • 8
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • C. Raiborg, H. Stenmark, The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 458, 445-452 (2009).
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 9
    • 58149103425 scopus 로고    scopus 로고
    • Functional reconstitution of ESCRT-III assembly and disassembly
    • S. Saksena, J. Wahlman, D. Teis, A. E. Johnson, S. D. Emr, Functional reconstitution of ESCRT-III assembly and disassembly. Cell 136, 97-109 (2009).
    • (2009) Cell , vol.136 , pp. 97-109
    • Saksena, S.1    Wahlman, J.2    Teis, D.3    Johnson, A.E.4    Emr, S.D.5
  • 10
    • 58149280810 scopus 로고    scopus 로고
    • In vitro budding of intralumenal vesicles into late endosomes is regulated by Alix and Tsg101
    • T. Falguières, P. P. Luyet, C. Bissig, C. C. Scott, M. C. Velluz, J. Gruenberg, In vitro budding of intralumenal vesicles into late endosomes is regulated by Alix and Tsg101. Mol. Biol. Cell 19, 4942-4955 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4942-4955
    • Falguières, T.1    Luyet, P.P.2    Bissig, C.3    Scott, C.C.4    Velluz, M.C.5    Gruenberg, J.6
  • 11
    • 30444456831 scopus 로고    scopus 로고
    • EGF stimulates annexin 1-dependent inward vesiculation in a multivesicular endosome subpopulation
    • I. J. White, L. M. Bailey, M. R. Aghakhani, S. E. Moss, C. E. Futter, EGF stimulates annexin 1-dependent inward vesiculation in a multivesicular endosome subpopulation. EMBO J. 25, 1-12 (2006).
    • (2006) EMBO J. , vol.25 , pp. 1-12
    • White, I.J.1    Bailey, L.M.2    Aghakhani, M.R.3    Moss, S.E.4    Futter, C.E.5
  • 12
    • 67249110996 scopus 로고    scopus 로고
    • Multivesicular endosome biogenesis in the absence of ESCRTs
    • S. Stuffers, C. Sem Wegner, H. Stenmark, A. Brech, Multivesicular endosome biogenesis in the absence of ESCRTs. Traffic 10, 925-937 (2009).
    • (2009) Traffic , vol.10 , pp. 925-937
    • Stuffers, S.1    Sem Wegner, C.2    Stenmark, H.3    Brech, A.4
  • 14
    • 3142592401 scopus 로고    scopus 로고
    • Not just a sink: Endosomes in control of signal transduction
    • M. Miaczynska, L. Pelkmans, M. Zerial, Not just a sink: Endosomes in control of signal transduction. Curr. Opin. Cell Biol. 16, 400-406 (2004).
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 400-406
    • Miaczynska, M.1    Pelkmans, L.2    Zerial, M.3
  • 15
    • 23044515099 scopus 로고    scopus 로고
    • Functions and mechanisms of retrograde neurotrophin signalling
    • L. S. Zweifel, R. Kuruvilla, D. D. Ginty, Functions and mechanisms of retrograde neurotrophin signalling. Nat. Rev. Neurosci. 6, 615-625 (2005).
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 615-625
    • Zweifel, L.S.1    Kuruvilla, R.2    Ginty, D.D.3
  • 16
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: Towards the systems level
    • A. Citri, Y. Yarden, EGF-ERBB signalling: Towards the systems level. Nat. Rev. Mol. Cell Biol. 7, 505-516 (2006).
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 17
    • 69249137477 scopus 로고    scopus 로고
    • Endocytosis and signalling: Intertwining molecular networks
    • A. Sorkin, M. von Zastrow, Endocytosis and signalling: Intertwining molecular networks. Nat. Rev. Mol. Cell Biol. 10, 609-622 (2009).
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 609-622
    • Sorkin, A.1    Von Zastrow, M.2
  • 18
    • 33644769212 scopus 로고    scopus 로고
    • Endocytosis conducts the cell signaling orchestra
    • S. Polo, P. P. Di Fiore, Endocytosis conducts the cell signaling orchestra. Cell 124, 897-900 (2006).
    • (2006) Cell , vol.124 , pp. 897-900
    • Polo, S.1    Di Fiore, P.P.2
  • 20
    • 80052622155 scopus 로고    scopus 로고
    • ESCRT proteins and cell signalling
    • C. S. Wegner, L. M. Rodahl, H. Stenmark, ESCRT proteins and cell signalling. Traffic 12, 1291-1297 (2011).
    • (2011) Traffic , vol.12 , pp. 1291-1297
    • Wegner, C.S.1    Rodahl, L.M.2    Stenmark, H.3
  • 21
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • A. V. Vieira, C. Lamaze, S. L. Schmid, Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 274, 2086-2089 (1996).
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 22
    • 48549088895 scopus 로고    scopus 로고
    • Clathrin-mediated internalization is essential for sustained EGFR signaling but dispensable for degradation
    • S. Sigismund, E. Argenzio, D. Tosoni, E. Cavallaro, S. Polo, P. P. Di Fiore, Clathrin-mediated internalization is essential for sustained EGFR signaling but dispensable for degradation. Dev. Cell 15, 209-219 (2008).
    • (2008) Dev. Cell , vol.15 , pp. 209-219
    • Sigismund, S.1    Argenzio, E.2    Tosoni, D.3    Cavallaro, E.4    Polo, S.5    Di Fiore, P.P.6
  • 23
    • 14544288669 scopus 로고    scopus 로고
    • The association of epsin with ubiquitinated cargo along the endocytic pathway is negatively regulated by its interaction with clathrin
    • H. Chen, P. De Camilli, The association of epsin with ubiquitinated cargo along the endocytic pathway is negatively regulated by its interaction with clathrin. Proc. Natl. Acad. Sci. U.S.A. 102, 2766-2771 (2005).
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 2766-2771
    • Chen, H.1    De Camilli, P.2
  • 25
    • 70350376635 scopus 로고    scopus 로고
    • Internalization and intracellular sorting of the EGF receptor: A model for understanding the mechanisms of receptor trafficking
    • I. H. Madshus, E. Stang, Internalization and intracellular sorting of the EGF receptor: A model for understanding the mechanisms of receptor trafficking. J. Cell Sci. 122, 3433-3439 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 3433-3439
    • Madshus, I.H.1    Stang, E.2
  • 27
    • 0027965262 scopus 로고
    • Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma
    • G. M. Di Guglielmo, P. C. Baass, W. J. Ou, B. I. Posner, J. J. Bergeron, Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma. EMBO J. 13, 4269-4277 (1994).
    • (1994) EMBO J. , vol.13 , pp. 4269-4277
    • Di Guglielmo, G.M.1    Baass, P.C.2    Ou, W.J.3    Posner, B.I.4    Bergeron, J.J.5
  • 28
    • 10744233838 scopus 로고    scopus 로고
    • Endocytosis and signaling: A relationship under development
    • M. González-Gaitán, H. Stenmark, Endocytosis and signaling: A relationship under development. Cell 115, 513-521 (2003).
    • (2003) Cell , vol.115 , pp. 513-521
    • González-Gaitán, M.1    Stenmark, H.2
  • 29
    • 0036899420 scopus 로고    scopus 로고
    • Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction
    • D. Teis, W. Wunderlich, L. A. Huber, Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction. Dev. Cell 3, 803-814 (2002).
    • (2002) Dev. Cell , vol.3 , pp. 803-814
    • Teis, D.1    Wunderlich, W.2    Huber, L.A.3
  • 30
    • 62049084764 scopus 로고    scopus 로고
    • The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes
    • S. Nada, A. Hondo, A. Kasai, M. Koike, K. Saito, Y. Uchiyama, M. Okada, The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes. EMBO J. 28, 477-489 (2009).
    • (2009) EMBO J. , vol.28 , pp. 477-489
    • Nada, S.1    Hondo, A.2    Kasai, A.3    Koike, M.4    Saito, K.5    Uchiyama, Y.6    Okada, M.7
  • 31
    • 0037040959 scopus 로고    scopus 로고
    • Selective in vivo inhibition of mitogen-activated protein kinase activation using cell-permeable peptides
    • B. R. Kelemen, K. Hsiao, S. A. Goueli, Selective in vivo inhibition of mitogen-activated protein kinase activation using cell-permeable peptides. J. Biol. Chem. 277, 8741-8748 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 8741-8748
    • Kelemen, B.R.1    Hsiao, K.2    Goueli, S.A.3
  • 32
    • 0024240990 scopus 로고
    • Blocking of EGF-dependent cell proliferation by EGF receptor kinase inhibitors
    • P. Yaish, A. Gazit, C. Gilon, A. Levitzki, Blocking of EGF-dependent cell proliferation by EGF receptor kinase inhibitors. Science 242, 933-935 (1988).
    • (1988) Science , vol.242 , pp. 933-935
    • Yaish, P.1    Gazit, A.2    Gilon, C.3    Levitzki, A.4
  • 33
    • 0029011218 scopus 로고
    • The MAPK signaling cascade
    • R. Seger, E. G. Krebs, The MAPK signaling cascade. FASEB J. 9, 726-735 (1995).
    • (1995) FASEB J. , vol.9 , pp. 726-735
    • Seger, R.1    Krebs, E.G.2
  • 34
    • 0037169336 scopus 로고    scopus 로고
    • Hrs regulates endosome membrane invagination and tyrosine kinase receptor signaling in Drosophila
    • T. E. Lloyd, R. Atkinson, M. N. Wu, Y. Zhou, G. Pennetta, H. J. Bellen, Hrs regulates endosome membrane invagination and tyrosine kinase receptor signaling in Drosophila. Cell 108, 261-269 (2002).
    • (2002) Cell , vol.108 , pp. 261-269
    • Lloyd, T.E.1    Atkinson, R.2    Wu, M.N.3    Zhou, Y.4    Pennetta, G.5    Bellen, H.J.6
  • 35
    • 0041488656 scopus 로고    scopus 로고
    • Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes
    • K. G. Bache, A. Brech, A. Mehlum, H. Stenmark, Hrs regulates multivesicular body formation via ESCRT recruitment to endosomes. J. Cell Biol. 162, 435-442 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 435-442
    • Bache, K.G.1    Brech, A.2    Mehlum, A.3    Stenmark, H.4
  • 36
    • 33745929286 scopus 로고    scopus 로고
    • Distinct roles for Tsg101 and Hrs in multivesicular body formation and inward vesiculation
    • M. Razi, C. E. Futter, Distinct roles for Tsg101 and Hrs in multivesicular body formation and inward vesiculation. Mol. Biol. Cell 17, 3469-3483 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3469-3483
    • Razi, M.1    Futter, C.E.2
  • 41
    • 23844481792 scopus 로고    scopus 로고
    • Depletion of TSG101 forms a mammalian "Class E" compartment: A multicisternal early endosome with multiple sorting defects
    • A. Doyotte, M. R. Russell, C. R. Hopkins, P. G. Woodman, Depletion of TSG101 forms a mammalian "Class E" compartment: A multicisternal early endosome with multiple sorting defects. J. Cell Sci. 118, 3003-3017 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 3003-3017
    • Doyotte, A.1    Russell, M.R.2    Hopkins, C.R.3    Woodman, P.G.4
  • 42
    • 77950863406 scopus 로고    scopus 로고
    • Molecular mechanism of multivesicular body biogenesis by ESCRT complexes
    • T. Wollert, J. H. Hurley, Molecular mechanism of multivesicular body biogenesis by ESCRT complexes. Nature 464, 864-869 (2010).
    • (2010) Nature , vol.464 , pp. 864-869
    • Wollert, T.1    Hurley, J.H.2
  • 44
    • 38849164882 scopus 로고    scopus 로고
    • Differential functions of Hrs and ESCRT proteins in endocytic membrane trafficking
    • C. Raiborg, L. Malerod, N. M. Pedersen, H. Stenmark, Differential functions of Hrs and ESCRT proteins in endocytic membrane trafficking. Exp. Cell Res. 314, 801-813 (2008).
    • (2008) Exp. Cell Res. , vol.314 , pp. 801-813
    • Raiborg, C.1    Malerod, L.2    Pedersen, N.M.3    Stenmark, H.4
  • 45
    • 78951489049 scopus 로고    scopus 로고
    • Feedback regulation of EGFR signalling: Decision making by early and delayed loops
    • R. Avraham, Y. Yarden, Feedback regulation of EGFR signalling: Decision making by early and delayed loops. Nat. Rev. Mol. Cell Biol. 12, 104-117 (2011).
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 104-117
    • Avraham, R.1    Yarden, Y.2
  • 49
    • 44049084101 scopus 로고    scopus 로고
    • The Bro1-related protein HD-PTP/PTPN23 is required for endosomal cargo sorting and multivesicular body morphogenesis
    • A. Doyotte, A. Mironov, E. McKenzie, P. Woodman, The Bro1-related protein HD-PTP/PTPN23 is required for endosomal cargo sorting and multivesicular body morphogenesis. Proc. Natl. Acad. Sci. U.S.A. 105, 6308-6313 (2008).
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6308-6313
    • Doyotte, A.1    Mironov, A.2    McKenzie, E.3    Woodman, P.4
  • 50
    • 56149121241 scopus 로고    scopus 로고
    • The ESCRT-I subunit TSG101 controls endosome-to-cytosol release of viral RNA
    • P. P. Luyet, T. Falguières, V. Pons, A. K. Pattnaik, J. Gruenberg, The ESCRT-I subunit TSG101 controls endosome-to-cytosol release of viral RNA. Traffic 9, 2279-2290 (2008).
    • (2008) Traffic , vol.9 , pp. 2279-2290
    • Luyet, P.P.1    Falguières, T.2    Pons, V.3    Pattnaik, A.K.4    Gruenberg, J.5
  • 51
    • 21644443846 scopus 로고    scopus 로고
    • Alix regulates cortical actin and the spatial distribution of endosomes
    • A. Cabezas, K. G. Bache, A. Brech, H. Stenmark, Alix regulates cortical actin and the spatial distribution of endosomes. J. Cell Sci. 118, 2625-2635 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 2625-2635
    • Cabezas, A.1    Bache, K.G.2    Brech, A.3    Stenmark, H.4
  • 52
    • 4744365071 scopus 로고    scopus 로고
    • Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex
    • M. H. Schmidt, D. Hoeller, J. Yu, F. B. Furnari, W. K. Cavenee, I. Dikic, O. Bogler, Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex. Mol. Cell. Biol. 24, 8981-8993 (2004).
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8981-8993
    • Schmidt, M.H.1    Hoeller, D.2    Yu, J.3    Furnari, F.B.4    Cavenee, W.K.5    Dikic, I.6    Bogler, O.7
  • 53
    • 63049107267 scopus 로고    scopus 로고
    • Systems biology of growth factor-induced receptor endocytosis
    • Y. Zwang, Y. Yarden, Systems biology of growth factor-induced receptor endocytosis. Traffic 10, 349-363 (2009).
    • (2009) Traffic , vol.10 , pp. 349-363
    • Zwang, Y.1    Yarden, Y.2
  • 54
    • 36749036679 scopus 로고    scopus 로고
    • EGF receptor ubiquitination is not necessary for its internalization
    • F. Huang, L. K. Goh, A. Sorkin, EGF receptor ubiquitination is not necessary for its internalization. Proc. Natl. Acad. Sci. U.S.A. 104, 16904-16909 (2007).
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 16904-16909
    • Huang, F.1    Goh, L.K.2    Sorkin, A.3
  • 55
  • 56
    • 42349108970 scopus 로고    scopus 로고
    • A tale of two Cbls: Interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation
    • S. Pennock, Z. Wang, A tale of two Cbls: Interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation. Mol. Cell. Biol. 28, 3020-3037 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3020-3037
    • Pennock, S.1    Wang, Z.2
  • 57
    • 67349158752 scopus 로고    scopus 로고
    • Molecular assemblies and membrane domains in multivesicular endosome dynamics
    • T. Falguières, P. P. Luyet, J. Gruenberg, Molecular assemblies and membrane domains in multivesicular endosome dynamics. Exp. Cell Res. 315, 1567-1573 (2009).
    • (2009) Exp. Cell Res. , vol.315 , pp. 1567-1573
    • Falguières, T.1    Luyet, P.P.2    Gruenberg, J.3
  • 58
    • 4744342856 scopus 로고    scopus 로고
    • Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation
    • L. M. Grøvdal, E. Stang, A. Sorkin, I. H. Madshus, Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation. Exp. Cell Res. 300, 388-395 (2004).
    • (2004) Exp. Cell Res. , vol.300 , pp. 388-395
    • Grøvdal, L.M.1    Stang, E.2    Sorkin, A.3    Madshus, I.H.4
  • 59
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • J. McCullough, M. J. Clague, S. Urbe, AMSH is an endosome-associated ubiquitin isopeptidase. J. Cell Biol. 166, 487-492 (2004).
    • (2004) J. Cell Biol. , vol.166 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbe, S.3
  • 60
    • 27644593284 scopus 로고    scopus 로고
    • Mutations in erupted, the Drosophila ortholog of mammalian tumor susceptibility gene 101, elicit non-cell-autonomous overgrowth
    • K. H. Moberg, S. Schelble, S. K. Burdick, I. K. Hariharan, Mutations in erupted, the Drosophila ortholog of mammalian tumor susceptibility gene 101, elicit non-cell-autonomous overgrowth. Dev. Cell 9, 699-710 (2005).
    • (2005) Dev. Cell , vol.9 , pp. 699-710
    • Moberg, K.H.1    Schelble, S.2    Burdick, S.K.3    Hariharan, I.K.4
  • 61
    • 27644498439 scopus 로고    scopus 로고
    • Tumor suppressor properties of the ESCRT-II complex component Vps25 in Drosophila
    • B. J. Thompson, J. Mathieu, H. H. Sung, E. Loeser, P. Rørth, S. M. Cohen, Tumor suppressor properties of the ESCRT-II complex component Vps25 in Drosophila. Dev. Cell 9, 711-720 (2005).
    • (2005) Dev. Cell , vol.9 , pp. 711-720
    • Thompson, B.J.1    Mathieu, J.2    Sung, H.H.3    Loeser, E.4    Rørth, P.5    Cohen, S.M.6
  • 62
    • 27644568520 scopus 로고    scopus 로고
    • The Drosophila tumor suppressor vps25 prevents nonautonomous overproliferation by regulating Notch trafficking
    • T. Vaccari, D. Bilder, The Drosophila tumor suppressor vps25 prevents nonautonomous overproliferation by regulating Notch trafficking. Dev. Cell 9, 687-698 (2005).
    • (2005) Dev. Cell , vol.9 , pp. 687-698
    • Vaccari, T.1    Bilder, D.2
  • 63
    • 0029904430 scopus 로고    scopus 로고
    • Tsg101: A novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells
    • L. Li, S. N. Cohen, tsg101: A novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells. Cell 85, 319-329 (1996).
    • (1996) Cell , vol.85 , pp. 319-329
    • Li, L.1    Cohen, S.N.2
  • 64
    • 44449127738 scopus 로고    scopus 로고
    • Endosomal sorting complex required for transport proteins in cancer pathogenesis, vesicular transport, and non-endosomal functions
    • N. Tanaka, M. Kyuuma, K. Sugamura, Endosomal sorting complex required for transport proteins in cancer pathogenesis, vesicular transport, and non-endosomal functions. Cancer Sci. 99, 1293-1303 (2008).
    • (2008) Cancer Sci. , vol.99 , pp. 1293-1303
    • Tanaka, N.1    Kyuuma, M.2    Sugamura, K.3
  • 66
    • 34347205268 scopus 로고    scopus 로고
    • Inhibition of tumor growth and metastasis by depletion of vesicular sorting protein Hrs: Its regulatory role on E-cadherin and β-catenin
    • M. Toyoshima, N. Tanaka, J. Aoki, Y. Tanaka, K. Murata, M. Kyuuma, H. Kobayashi, N. Ishii, N. Yaegashi, K. Sugamura, Inhibition of tumor growth and metastasis by depletion of vesicular sorting protein Hrs: Its regulatory role on E-cadherin and β-catenin. Cancer Res. 67, 5162-5171 (2007).
    • (2007) Cancer Res. , vol.67 , pp. 5162-5171
    • Toyoshima, M.1    Tanaka, N.2    Aoki, J.3    Tanaka, Y.4    Murata, K.5    Kyuuma, M.6    Kobayashi, H.7    Ishii, N.8    Yaegashi, N.9    Sugamura, K.10
  • 67
    • 0023677140 scopus 로고
    • Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytic system
    • H. S. Wiley, Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytic system. J. Cell Biol. 107, 801-810 (1988).
    • (1988) J. Cell Biol. , vol.107 , pp. 801-810
    • Wiley, H.S.1
  • 68
    • 0025160570 scopus 로고
    • Quantitative analysis of the endocytic system involved in hormone-induced receptor internalization
    • K. A. Lund, L. K. Opresko, C. Starbuck, B. J. Walsh, H. S. Wiley, Quantitative analysis of the endocytic system involved in hormone-induced receptor internalization. J. Biol. Chem. 265, 15713-15723 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 15713-15723
    • Lund, K.A.1    Opresko, L.K.2    Starbuck, C.3    Walsh, B.J.4    Wiley, H.S.5
  • 69
    • 62649159446 scopus 로고    scopus 로고
    • Endocytosis and intracellular trafficking of ErbBs
    • A. Sorkin, L. K. Goh, Endocytosis and intracellular trafficking of ErbBs. Exp. Cell Res. 315, 683-696 (2009).
    • (2009) Exp. Cell Res. , vol.315 , pp. 683-696
    • Sorkin, A.1    Goh, L.K.2
  • 70
    • 0028483678 scopus 로고
    • EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor
    • S. Traverse, K. Seedorf, H. Paterson, C. J. Marshall, P. Cohen, A. Ullrich, EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor. Curr. Biol. 4, 694-701 (1994).
    • (1994) Curr. Biol. , vol.4 , pp. 694-701
    • Traverse, S.1    Seedorf, K.2    Paterson, H.3    Marshall, C.J.4    Cohen, P.5    Ullrich, A.6
  • 71
    • 63749086305 scopus 로고    scopus 로고
    • ErbB receptors and signaling pathways in cancer
    • N. E. Hynes, G. MacDonald, ErbB receptors and signaling pathways in cancer. Curr. Opin. Cell Biol. 21, 177-184 (2009).
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 177-184
    • Hynes, N.E.1    MacDonald, G.2
  • 73
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M. M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 74
    • 0014195281 scopus 로고
    • Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels
    • A. L. Shapiro, E. Viñuela, J. V. Maizel Jr., Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem. Biophys. Res. Commun. 28, 815-820 (1967).
    • (1967) Biochem. Biophys. Res. Commun. , vol.28 , pp. 815-820
    • Shapiro, A.L.1    Viñuela, E.2    Maizel Jr., J.V.3
  • 75
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U. K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 76
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • H. Towbin, T. Staehelin, J. Gordon, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76, 4350-4354 (1979).
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 77
    • 0019551730 scopus 로고
    • "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • W. N. Burnette, "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112, 195-203 (1981).
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 78
    • 0030812588 scopus 로고    scopus 로고
    • Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes
    • F. Gu, F. Aniento, R. G. Parton, J. Gruenberg, Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes. J. Cell Biol. 139, 1183-1195 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 1183-1195
    • Gu, F.1    Aniento, F.2    Parton, R.G.3    Gruenberg, J.4
  • 79
    • 0032510559 scopus 로고    scopus 로고
    • A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
    • T. Kobayashi, E. Stang, K. S. Fang, P. de Moerloose, R. G. Parton, J. Gruenberg, A lipid associated with the antiphospholipid syndrome regulates endosome structure and function. Nature 392, 193-197 (1998).
    • (1998) Nature , vol.392 , pp. 193-197
    • Kobayashi, T.1    Stang, E.2    Fang, K.S.3    De Moerloose, P.4    Parton, R.G.5    Gruenberg, J.6
  • 83
    • 79251648880 scopus 로고    scopus 로고
    • Orientation and expression of methicillin-resistant Staphylococcus aureus small RNAs by direct multiplexed measurements using the nCounter of NanoString technology
    • M. Beaume, D. Hernandez, M. Docquier, C. Delucinge-Vivier, P. Descombes, P. Francois, Orientation and expression of methicillin-resistant Staphylococcus aureus small RNAs by direct multiplexed measurements using the nCounter of NanoString technology. J. Microbiol. Methods 84, 327-334 (2011).
    • (2011) J. Microbiol. Methods , vol.84 , pp. 327-334
    • Beaume, M.1    Hernandez, D.2    Docquier, M.3    Delucinge-Vivier, C.4    Descombes, P.5    Francois, P.6
  • 84
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • RESEARCH0034
    • J. Vandesompele, K. De Preter, F. Pattyn, B. Poppe, N. Van Roy, A. De Paepe, F. Speleman, Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol. 3, RESEARCH0034 (2002).
    • (2002) Genome Biol. , vol.3
    • Vandesompele, J.1    De Preter, K.2    Pattyn, F.3    Poppe, B.4    Van Roy, N.5    De Paepe, A.6    Speleman, F.7


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