메뉴 건너뛰기




Volumn 25, Issue 24, 2005, Pages 11005-11018

Endosomal transport of ErbB-2: Mechanism for nuclear entry of the cell surface receptor

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; DYNAMIN; EPIDERMAL GROWTH FACTOR RECEPTOR 2; GUANOSINE TRIPHOSPHATASE; KARYOPHERIN BETA; MUTANT PROTEIN; NUCLEOPORIN; OLIGONUCLEOTIDE; PROTEIN NUP358; PROTEIN TYROSINE KINASE; RAN PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 28544448741     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.24.11005-11018.2005     Document Type: Article
Times cited : (201)

References (57)
  • 1
    • 0026899636 scopus 로고
    • A ligand for the erbB-2 oncogene product (GP30) induces differentiation of human breast cancer cells
    • Bacus, S. S., E. Huberman, D. Chin, K. Kiguchi, S. Simpson, M. Lippman, and R. Lupu. 1992. A ligand for the erbB-2 oncogene product (GP30) induces differentiation of human breast cancer cells. Cell Growth Differ. 3:401-411.
    • (1992) Cell Growth Differ. , vol.3 , pp. 401-411
    • Bacus, S.S.1    Huberman, E.2    Chin, D.3    Kiguchi, K.4    Simpson, S.5    Lippman, M.6    Lupu, R.7
  • 2
    • 0035931750 scopus 로고    scopus 로고
    • Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import
    • Ben-Efraim, I., and L. Gerace. 2001. Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import. J. Cell Biol. 152:411-417.
    • (2001) J. Cell Biol. , vol.152 , pp. 411-417
    • Ben-Efraim, I.1    Gerace, L.2
  • 5
    • 0036646099 scopus 로고    scopus 로고
    • Cytoplasmic transport of Stat3 by receptor-mediated endocytosis
    • Bild, A. H., J. Turkson, and R. Jove. 2002. Cytoplasmic transport of Stat3 by receptor-mediated endocytosis. EMBO J. 21:3255-3263.
    • (2002) EMBO J. , vol.21 , pp. 3255-3263
    • Bild, A.H.1    Turkson, J.2    Jove, R.3
  • 6
    • 0031720535 scopus 로고    scopus 로고
    • Differential distribution of dynamin isoforms in mammalian cells
    • Cao, H., F. Garcia, and M. A. McNiven. 1998. Differential distribution of dynamin isoforms in mammalian cells. Mol. Biol. Cell 9:2595-2609.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2595-2609
    • Cao, H.1    Garcia, F.2    McNiven, M.A.3
  • 7
    • 0034094514 scopus 로고    scopus 로고
    • Disruption of Golgi structure and function in mammalian cells expressing a mutant dynamin
    • Cao, H., H. M. Thompson, E. W. Krueger, and M. A. McNiven. 2000. Disruption of Golgi structure and function in mammalian cells expressing a mutant dynamin. J. Cell Sci. 113:1993-2002.
    • (2000) J. Cell Sci. , vol.113 , pp. 1993-2002
    • Cao, H.1    Thompson, H.M.2    Krueger, E.W.3    McNiven, M.A.4
  • 8
    • 0037377217 scopus 로고    scopus 로고
    • Nuclear localization and possible functions of receptor tyrosine kinases
    • Carpenter, G. 2003. Nuclear localization and possible functions of receptor tyrosine kinases. Curr. Opin. Cell Biol. 15:143-148.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 143-148
    • Carpenter, G.1
  • 10
    • 0032579263 scopus 로고    scopus 로고
    • Eps15R is a tyrosine kinase substrate with characteristics of a docking protein possibly involved in coated pits-mediated internalization
    • Coda, L., A. E. Salcini, S. Confalonieri, G. Pelicci, T. Sorkina, A. Sorkin, P. G. Pelicci, and P. P. Di Fiore. 1998. Eps15R is a tyrosine kinase substrate with characteristics of a docking protein possibly involved in coated pits-mediated internalization. J. Biol. Chem. 273:3003-3012.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3003-3012
    • Coda, L.1    Salcini, A.E.2    Confalonieri, S.3    Pelicci, G.4    Sorkina, T.5    Sorkin, A.6    Pelicci, P.G.7    Di Fiore, P.P.8
  • 11
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner, S. D., and S. L. Schmid. 2003. Regulated portals of entry into the cell. Nature 422:37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 12
    • 0033611126 scopus 로고    scopus 로고
    • The eps15 homology (EH) domain-based interaction between eps15 and hrb connects the molecular machinery of endocytosis to that of nucleocytosolic transport
    • Doria, M., A. E. Salcini, E. Colombo, T. G. Parslow, P. G. Pelicci, and P. P. Di Fiore. 1999. The eps15 homology (EH) domain-based interaction between eps15 and hrb connects the molecular machinery of endocytosis to that of nucleocytosolic transport. J. Cell Biol. 147:1379-1384.
    • (1999) J. Cell Biol. , vol.147 , pp. 1379-1384
    • Doria, M.1    Salcini, A.E.2    Colombo, E.3    Parslow, T.G.4    Pelicci, P.G.5    Di Fiore, P.P.6
  • 13
    • 0033525718 scopus 로고    scopus 로고
    • VEGF induces nuclear translocation of Flk-1/KDR, endothelial nitric oxide synthase, and caveolin-1 in vascular endothelial cells
    • Feng, Y., V. J. Venema, R. C. Venema, N. Tsai, and R. B. Caldwell. 1999. VEGF induces nuclear translocation of Flk-1/KDR, endothelial nitric oxide synthase, and caveolin-1 in vascular endothelial cells. Biochem. Biophys. Res. Commun. 256:192-197.
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 192-197
    • Feng, Y.1    Venema, V.J.2    Venema, R.C.3    Tsai, N.4    Caldwell, R.B.5
  • 14
    • 0031724593 scopus 로고    scopus 로고
    • Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6
    • Freedman, D. A., and A. J. Levine. 1998. Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6. Mol. Cell. Biol. 18:7288-7293.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7288-7293
    • Freedman, D.A.1    Levine, A.J.2
  • 15
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich, D., and U. Kutay. 1999. Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15:607-660.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 19
    • 0033953587 scopus 로고    scopus 로고
    • A nuclear export signal in the N-terminal regulatory domain of IκBα controls cytoplasmic localization of inactive NF-κB/IκBα complexes
    • Huang, T. T., N. Kudo, M. Yoshida, and S. Miyamoto. 2000. A nuclear export signal in the N-terminal regulatory domain of IκBα controls cytoplasmic localization of inactive NF-κB/IκBα complexes. Proc. Natl. Acad. Sci. USA 97:1014-1019.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1014-1019
    • Huang, T.T.1    Kudo, N.2    Yoshida, M.3    Miyamoto, S.4
  • 21
    • 0041970961 scopus 로고    scopus 로고
    • Vascular endothelial growth factor expression, beta-catenin tyrosine phosphorylation, and endothelial proliferative behavior: A pathway for transformation?
    • Ilan, N., A. Tucker, and J. A. Madri. 2003. Vascular endothelial growth factor expression, beta-catenin tyrosine phosphorylation, and endothelial proliferative behavior: a pathway for transformation? Lab. Investig. 83:1105-1115.
    • (2003) Lab. Investig. , vol.83 , pp. 1105-1115
    • Ilan, N.1    Tucker, A.2    Madri, J.A.3
  • 23
    • 0029559922 scopus 로고
    • Fibroblast growth factor receptors (FGFRs) localize in different cellular compartments. A splice variant of FGFR-3 localizes to the nucleus
    • Johnston, C. L., H. C. Cox, J. J. Gomm, and R. C. Coombes. 1995. Fibroblast growth factor receptors (FGFRs) localize in different cellular compartments. A splice variant of FGFR-3 localizes to the nucleus. J. Biol. Chem. 270: 30643-30650.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30643-30650
    • Johnston, C.L.1    Cox, H.C.2    Gomm, J.J.3    Coombes, R.C.4
  • 24
    • 0032488987 scopus 로고    scopus 로고
    • The nuclear LIM domain interactor NLI mediates homo- and heterodimerization of LIM domain transcription factors
    • Jurata, L. W., S. L. Pfaff, and G. N. Gill. 1998. The nuclear LIM domain interactor NLI mediates homo- and heterodimerization of LIM domain transcription factors. J. Biol. Chem. 273:3152-3157.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3152-3157
    • Jurata, L.W.1    Pfaff, S.L.2    Gill, G.N.3
  • 26
    • 0028968949 scopus 로고
    • Tyrosine kinase inhibition: An approach to drug development
    • Levitzki, A., and A. Gazit. 1995. Tyrosine kinase inhibition: an approach to drug development. Science 267:1782-1788.
    • (1995) Science , vol.267 , pp. 1782-1788
    • Levitzki, A.1    Gazit, A.2
  • 29
    • 11244280137 scopus 로고    scopus 로고
    • Novel prognostic value of nuclear epidermal growth factor receptor in breast cancer
    • Lo, H. W., W. Xia, Y. Wei, M. Ali-Seyed, S. F. Huang, and M. C. Hung. 2005. Novel prognostic value of nuclear epidermal growth factor receptor in breast cancer. Cancer Res. 65:338-348.
    • (2005) Cancer Res , vol.65 , pp. 338-348
    • Lo, H.W.1    Xia, W.2    Wei, Y.3    Ali-Seyed, M.4    Huang, S.F.5    Hung, M.C.6
  • 30
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • Macara, I. G. 2001. Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 65:570-594.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 570-594
    • Macara, I.G.1
  • 31
    • 0029954235 scopus 로고    scopus 로고
    • Nuclear translocation of fibroblast growth factor (FGF) receptors in response to FGF-2
    • Maher, P. A. 1996. Nuclear translocation of fibroblast growth factor (FGF) receptors in response to FGF-2. J. Cell Biol. 134:529-536.
    • (1996) J. Cell Biol. , vol.134 , pp. 529-536
    • Maher, P.A.1
  • 32
    • 0034069067 scopus 로고    scopus 로고
    • The nuclear accumulation of a variant epidermal growth factor receptor (EGFR) lacking the transmembrane domain requires coexpression of a full-length EGFR
    • Marti, U., and A. Wells. 2000. The nuclear accumulation of a variant epidermal growth factor receptor (EGFR) lacking the transmembrane domain requires coexpression of a full-length EGFR. Mol. Cell Biol. Res. Commun. 3:8-14.
    • (2000) Mol. Cell Biol. Res. Commun. , vol.3 , pp. 8-14
    • Marti, U.1    Wells, A.2
  • 33
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The soluble phase
    • Mattaj, I. W., and L. Englmeier. 1998. Nucleocytoplasmic transport: the soluble phase. Annu. Rev. Biochem. 67:265-306.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 34
    • 0035816587 scopus 로고    scopus 로고
    • Vascular endothelial cell growth factor activates CRE-binding protein by signaling through the KDR receptor tyrosine kinase
    • Mayo, L. D., K. M. Kessler, R. Pincheira, R. S. Warren, and D. B. Donner. 2001. Vascular endothelial cell growth factor activates CRE-binding protein by signaling through the KDR receptor tyrosine kinase. J. Biol. Chem. 276:25184-25189.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25184-25189
    • Mayo, L.D.1    Kessler, K.M.2    Pincheira, R.3    Warren, R.S.4    Donner, D.B.5
  • 35
  • 36
    • 0035824391 scopus 로고    scopus 로고
    • γ-secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • Ni, C. Y., M. P. Murphy, T. E. Golde, and G. Carpenter. 2001. γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science 294:2179-2181.
    • (2001) Science , vol.294 , pp. 2179-2181
    • Ni, C.Y.1    Murphy, M.P.2    Golde, T.E.3    Carpenter, G.4
  • 39
    • 0027219132 scopus 로고
    • Elk-1 proteins are phosphoproteins and activators of mitogen-activated protein kinase
    • Rao, V. N., and E. S. Reddy. 1993. Elk-1 proteins are phosphoproteins and activators of mitogen-activated protein kinase. Cancer Res. 53:3449-3454.
    • (1993) Cancer Res. , vol.53 , pp. 3449-3454
    • Rao, V.N.1    Reddy, E.S.2
  • 40
    • 0035911965 scopus 로고    scopus 로고
    • Importin beta-mediated nuclear import of fibroblast growth factor receptor: Role in cell proliferation
    • Reilly, J. F., and P. A. Maher. 2001. Importin beta-mediated nuclear import of fibroblast growth factor receptor: role in cell proliferation. J. Cell Biol. 152:1307-1312.
    • (2001) J. Cell Biol. , vol.152 , pp. 1307-1312
    • Reilly, J.F.1    Maher, P.A.2
  • 41
    • 0037757726 scopus 로고    scopus 로고
    • Nuclear matrix association of insulin receptor and IRS-1 by insulin in osteoblast-like UMR-106 cells
    • Seol, K. C., and S. J. Kim. 2003. Nuclear matrix association of insulin receptor and IRS-1 by insulin in osteoblast-like UMR-106 cells. Biochem. Biophys. Res. Commun. 306:898-904.
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 898-904
    • Seol, K.C.1    Kim, S.J.2
  • 42
    • 0036701910 scopus 로고    scopus 로고
    • Dynamin and endocytosis
    • Sever, S. 2002. Dynamin and endocytosis. Curr. Opin. Cell Biol. 14:463-467.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 463-467
    • Sever, S.1
  • 43
    • 0037347399 scopus 로고    scopus 로고
    • cAMP-induced differentiation of human neuronal progenitor cells is mediated by nuclear fibroblast growth factor receptor-1 (FGFR1)
    • Stachowiak, E. K., X. Fang, J. Myers, S. Dunham, and M. K. Stachowiak. 2003. cAMP-induced differentiation of human neuronal progenitor cells is mediated by nuclear fibroblast growth factor receptor-1 (FGFR1). J. Neurochem. 84:1296-1312.
    • (2003) J. Neurochem. , vol.84 , pp. 1296-1312
    • Stachowiak, E.K.1    Fang, X.2    Myers, J.3    Dunham, S.4    Stachowiak, M.K.5
  • 44
    • 0031001129 scopus 로고    scopus 로고
    • Nuclear accumulation of fibroblast growth factor receptors in human glial cells-association with cell proliferation
    • Stachowiak, E. K., P. A. Maher, J. Tucholski, E. Mordechal, A. Joy, J. Moffett, S. Coons, and M. K. Stachowiak. 1997. Nuclear accumulation of fibroblast growth factor receptors in human glial cells-association with cell proliferation. Oncogene 14:2201-2211.
    • (1997) Oncogene , vol.14 , pp. 2201-2211
    • Stachowiak, E.K.1    Maher, P.A.2    Tucholski, J.3    Mordechal, E.4    Joy, A.5    Moffett, J.6    Coons, S.7    Stachowiak, M.K.8
  • 45
    • 0029785143 scopus 로고    scopus 로고
    • Nuclear accumulation of fibroblast growth factor receptors is regulated by multiple signals in adrenal medullary cells
    • Stachowiak, M. K., P. A. Maher, A. Joy, E. Mordechal, and E. K. Stachowiak. 1996. Nuclear accumulation of fibroblast growth factor receptors is regulated by multiple signals in adrenal medullary cells. Mol. Biol. Cell 7:1299-1317.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1299-1317
    • Stachowiak, M.K.1    Maher, P.A.2    Joy, A.3    Mordechal, E.4    Stachowiak, E.K.5
  • 46
    • 0034913423 scopus 로고    scopus 로고
    • Importin-beta-like nuclear transport receptors
    • Strom, A. C., and K. Weis. 2001. Importin-beta-like nuclear transport receptors. Genome Biol. 2:3008.1-3008.9.
    • (2001) Genome Biol. , vol.2
    • Strom, A.C.1    Weis, K.2
  • 47
    • 0037604556 scopus 로고    scopus 로고
    • Peering through the pore: Nuclear pore complex structure, assembly, and function
    • Suntharalingam, M., and S. R. Wente. 2003. Peering through the pore: nuclear pore complex structure, assembly, and function. Dev. Cell 4:775-789.
    • (2003) Dev. Cell , vol.4 , pp. 775-789
    • Suntharalingam, M.1    Wente, S.R.2
  • 50
    • 0036591883 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Cargo trafficking across the border
    • Weis, K. 2002. Nucleocytoplasmic transport: cargo trafficking across the border. Curr. Opin. Cell Biol. 14:328-335.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 328-335
    • Weis, K.1
  • 51
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle
    • Weis, K. 2003. Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell 112:441-451.
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 52
    • 0036727023 scopus 로고    scopus 로고
    • Signalling shortcuts: Cell-surface receptors in the nucleus?
    • Wells, A., and U. Marti. 2002. Signalling shortcuts: cell-surface receptors in the nucleus? Nat. Rev. Mol. Cell Biol. 3:697-702.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 697-702
    • Wells, A.1    Marti, U.2
  • 53
    • 0029070074 scopus 로고
    • Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin a homologous domain, and a leucine-rich region
    • Wu, J., M. J. Matunis, D. Kraemer, G. Blobel, and E. Coutavas. 1995. Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region. J. Biol. Chem. 270:14209-14213.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14209-14213
    • Wu, J.1    Matunis, M.J.2    Kraemer, D.3    Blobel, G.4    Coutavas, E.5
  • 54
    • 0028170686 scopus 로고
    • Nuclear localization of p185neu tyrosine kinase and its association with transcriptional transactivation
    • Xie, Y., and M. C. Hung. 1994. Nuclear localization of p185neu tyrosine kinase and its association with transcriptional transactivation. Biochem. Biophys. Res. Commun. 203:1589-1598.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1589-1598
    • Xie, Y.1    Hung, M.C.2
  • 55
    • 0032528001 scopus 로고    scopus 로고
    • Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1
    • Yang, J., E. S. Bardes, J. D. Moore, J. Brennan, M. A. Powers, and S. Kornbluth. 1998. Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1. Genes Dev. 12:2131-2143.
    • (1998) Genes Dev. , vol.12 , pp. 2131-2143
    • Yang, J.1    Bardes, E.S.2    Moore, J.D.3    Brennan, J.4    Powers, M.A.5    Kornbluth, S.6
  • 57
    • 0035040448 scopus 로고    scopus 로고
    • Altered intracellular localization of fibroblast growth factor receptor 3 in human breast cancer
    • Zammit, C., R. Barnard, J. Gomm, R. Coope, S. Shousha, C. Coombes, and C. Johnston. 2001. Altered intracellular localization of fibroblast growth factor receptor 3 in human breast cancer. J. Pathol. 194:27-34.
    • (2001) J. Pathol. , vol.194 , pp. 27-34
    • Zammit, C.1    Barnard, R.2    Gomm, J.3    Coope, R.4    Shousha, S.5    Coombes, C.6    Johnston, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.