메뉴 건너뛰기




Volumn 23, Issue 2, 2012, Pages 165-171

Nuclear translocation and functions of growth factor receptors

Author keywords

Cancer; Chromatin; Drug response; Endocytosis; Growth factors; Transcription

Indexed keywords

CELL SURFACE RECEPTOR; EPHRIN RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR 2; EPIDERMAL GROWTH FACTOR RECEPTOR 3; EPIDERMAL GROWTH FACTOR RECEPTOR 4; INSULIN RECEPTOR; SOMATOMEDIN C; VASCULOTROPIN RECEPTOR 1;

EID: 84858800071     PISSN: 10849521     EISSN: 10963634     Source Type: Journal    
DOI: 10.1016/j.semcdb.2011.09.004     Document Type: Review
Times cited : (11)

References (85)
  • 1
    • 34548456964 scopus 로고    scopus 로고
    • The interplay between clathrin-coated vesicles and cell signalling
    • Mills I.G. The interplay between clathrin-coated vesicles and cell signalling. Semin Cell Dev Biol 2007, 18:459-470.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 459-470
    • Mills, I.G.1
  • 3
    • 33646378439 scopus 로고    scopus 로고
    • The developing role of receptors and adaptors
    • Massie C., Mills I.G. The developing role of receptors and adaptors. Nat Rev Cancer 2006, 6:403-409.
    • (2006) Nat Rev Cancer , vol.6 , pp. 403-409
    • Massie, C.1    Mills, I.G.2
  • 5
    • 0023145865 scopus 로고
    • Translocation of epidermal growth factor to the hepatocyte nucleus during rat liver regeneration
    • Raper S.E., Burwen S.J., Barker M.E., Jones A.L. Translocation of epidermal growth factor to the hepatocyte nucleus during rat liver regeneration. Gastroenterology 1987, 92:1243-1250.
    • (1987) Gastroenterology , vol.92 , pp. 1243-1250
    • Raper, S.E.1    Burwen, S.J.2    Barker, M.E.3    Jones, A.L.4
  • 6
    • 0036614697 scopus 로고    scopus 로고
    • A novel mechanism for mitogenic signaling via pro-transforming growth factor alpha within hepatocyte nuclei
    • Grasl-Kraupp B., Schausberger E., Hufnagl K., Gerner C., Low-Baselli A., Rossmanith W., et al. A novel mechanism for mitogenic signaling via pro-transforming growth factor alpha within hepatocyte nuclei. Hepatology 2002, 35:1372-1380.
    • (2002) Hepatology , vol.35 , pp. 1372-1380
    • Grasl-Kraupp, B.1    Schausberger, E.2    Hufnagl, K.3    Gerner, C.4    Low-Baselli, A.5    Rossmanith, W.6
  • 7
    • 24744449739 scopus 로고    scopus 로고
    • Radiation-induced epidermal growth factor receptor nuclear import is linked to activation of DNA-dependent protein kinase
    • Dittmann K., Mayer C., Fehrenbacher B., Schaller M., Raju U., Milas L., et al. Radiation-induced epidermal growth factor receptor nuclear import is linked to activation of DNA-dependent protein kinase. J Biol Chem 2005, 280:31182-31189.
    • (2005) J Biol Chem , vol.280 , pp. 31182-31189
    • Dittmann, K.1    Mayer, C.2    Fehrenbacher, B.3    Schaller, M.4    Raju, U.5    Milas, L.6
  • 8
    • 67749093100 scopus 로고    scopus 로고
    • Ultraviolet irradiation-induces epidermal growth factor receptor (EGFR) nuclear translocation in human keratinocytes
    • Xu Y., Shao Y., Zhou J., Voorhees J.J., Fisher G.J. Ultraviolet irradiation-induces epidermal growth factor receptor (EGFR) nuclear translocation in human keratinocytes. J Cell Biochem 2009, 107:873-880.
    • (2009) J Cell Biochem , vol.107 , pp. 873-880
    • Xu, Y.1    Shao, Y.2    Zhou, J.3    Voorhees, J.J.4    Fisher, G.J.5
  • 9
    • 79551510855 scopus 로고    scopus 로고
    • EGFR nuclear translocation modulates DNA repair following cisplatin and ionizing radiation treatment
    • Liccardi G., Hartley J.A., Hochhauser D. EGFR nuclear translocation modulates DNA repair following cisplatin and ionizing radiation treatment. Cancer Res 2011, 71:1103-1114.
    • (2011) Cancer Res , vol.71 , pp. 1103-1114
    • Liccardi, G.1    Hartley, J.A.2    Hochhauser, D.3
  • 10
    • 79960379461 scopus 로고    scopus 로고
    • Nuclear epidermal growth factor receptor modulates cellular radio-sensitivity by regulation of chromatin access
    • Dittmann K., Mayer C., Fehrenbacher B., Schaller M., Kehlbach R., Rodemann H.P. Nuclear epidermal growth factor receptor modulates cellular radio-sensitivity by regulation of chromatin access. Radiother Oncol 2011, 99:317-322.
    • (2011) Radiother Oncol , vol.99 , pp. 317-322
    • Dittmann, K.1    Mayer, C.2    Fehrenbacher, B.3    Schaller, M.4    Kehlbach, R.5    Rodemann, H.P.6
  • 11
    • 77956939857 scopus 로고    scopus 로고
    • Nuclear EGFR shuttling induced by ionizing radiation is regulated by phosphorylation at residue Thr654
    • Dittmann K., Mayer C., Fehrenbacher B., Schaller M., Kehlbach R., Rodemann H.P. Nuclear EGFR shuttling induced by ionizing radiation is regulated by phosphorylation at residue Thr654. FEBS Lett 2010, 584:3878-3884.
    • (2010) FEBS Lett , vol.584 , pp. 3878-3884
    • Dittmann, K.1    Mayer, C.2    Fehrenbacher, B.3    Schaller, M.4    Kehlbach, R.5    Rodemann, H.P.6
  • 12
    • 75649095683 scopus 로고    scopus 로고
    • Nuclear EGFR as novel therapeutic target: insights into nuclear translocation and function
    • Dittmann K., Mayer C., Rodemann H.P. Nuclear EGFR as novel therapeutic target: insights into nuclear translocation and function. Strahlenther Onkol 2010, 186:1-6.
    • (2010) Strahlenther Onkol , vol.186 , pp. 1-6
    • Dittmann, K.1    Mayer, C.2    Rodemann, H.P.3
  • 13
    • 40249109168 scopus 로고    scopus 로고
    • Activation of protein kinase Cepsilon stimulates DNA-repair via epidermal growth factor receptor nuclear accumulation
    • Wanner G., Mayer C., Kehlbach R., Rodemann H.P., Dittmann K. Activation of protein kinase Cepsilon stimulates DNA-repair via epidermal growth factor receptor nuclear accumulation. Radiother Oncol 2008, 86:383-390.
    • (2008) Radiother Oncol , vol.86 , pp. 383-390
    • Wanner, G.1    Mayer, C.2    Kehlbach, R.3    Rodemann, H.P.4    Dittmann, K.5
  • 14
    • 34347223656 scopus 로고    scopus 로고
    • Somatic mutations in the tyrosine kinase domain of epidermal growth factor receptor (EGFR) abrogate EGFR-mediated radioprotection in non-small cell lung carcinoma
    • Das A.K., Chen B.P., Story M.D., Sato M., Minna J.D., Chen D.J., et al. Somatic mutations in the tyrosine kinase domain of epidermal growth factor receptor (EGFR) abrogate EGFR-mediated radioprotection in non-small cell lung carcinoma. Cancer Res 2007, 67:5267-5274.
    • (2007) Cancer Res , vol.67 , pp. 5267-5274
    • Das, A.K.1    Chen, B.P.2    Story, M.D.3    Sato, M.4    Minna, J.D.5    Chen, D.J.6
  • 15
    • 20444423286 scopus 로고    scopus 로고
    • Nuclear interaction of EGFR and STAT3 in the activation of the iNOS/NO pathway
    • Lo H.W., Hsu S.C., Ali-Seyed M., Gunduz M., Xia W., Wei Y., et al. Nuclear interaction of EGFR and STAT3 in the activation of the iNOS/NO pathway. Cancer Cell 2005, 7:575-589.
    • (2005) Cancer Cell , vol.7 , pp. 575-589
    • Lo, H.W.1    Hsu, S.C.2    Ali-Seyed, M.3    Gunduz, M.4    Xia, W.5    Wei, Y.6
  • 16
    • 79957982003 scopus 로고    scopus 로고
    • Nuclear translocation of epidermal growth factor receptor by Akt-dependent phosphorylation enhances breast cancer-resistant protein expression in gefitinib-resistant cells
    • Huang W.C., Chen Y.J., Li L.Y., Wei Y.L., Hsu S.C., Tsai S.L., et al. Nuclear translocation of epidermal growth factor receptor by Akt-dependent phosphorylation enhances breast cancer-resistant protein expression in gefitinib-resistant cells. J Biol Chem 2011, 286:20558-20568.
    • (2011) J Biol Chem , vol.286 , pp. 20558-20568
    • Huang, W.C.1    Chen, Y.J.2    Li, L.Y.3    Wei, Y.L.4    Hsu, S.C.5    Tsai, S.L.6
  • 17
    • 77953442037 scopus 로고    scopus 로고
    • Nuclear EGFR is required for cisplatin resistance and DNA repair
    • Hsu S.C., Miller S.A., Wang Y., Hung M.C. Nuclear EGFR is required for cisplatin resistance and DNA repair. Am J Transl Res 2009, 1:249-258.
    • (2009) Am J Transl Res , vol.1 , pp. 249-258
    • Hsu, S.C.1    Miller, S.A.2    Wang, Y.3    Hung, M.C.4
  • 18
    • 67249115311 scopus 로고    scopus 로고
    • Endocytic regulation of notch signalling during development
    • Furthauer M., Gonzalez-Gaitan M. Endocytic regulation of notch signalling during development. Traffic 2009, 10:792-802.
    • (2009) Traffic , vol.10 , pp. 792-802
    • Furthauer, M.1    Gonzalez-Gaitan, M.2
  • 19
    • 65549121943 scopus 로고    scopus 로고
    • Notch signaling: the core pathway and its posttranslational regulation
    • Fortini M.E. Notch signaling: the core pathway and its posttranslational regulation. Dev Cell 2009, 16:633-647.
    • (2009) Dev Cell , vol.16 , pp. 633-647
    • Fortini, M.E.1
  • 20
    • 0003356476 scopus 로고    scopus 로고
    • Role of the ErbB-4 carboxyl terminus in gamma-secretase cleavage
    • Ni C.Y., Yuan H., Carpenter G. Role of the ErbB-4 carboxyl terminus in gamma-secretase cleavage. J Biol Chem 2003, 278:4561-4565.
    • (2003) J Biol Chem , vol.278 , pp. 4561-4565
    • Ni, C.Y.1    Yuan, H.2    Carpenter, G.3
  • 21
    • 33645277094 scopus 로고    scopus 로고
    • Metalloproteinase/Presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling
    • Georgakopoulos A., Litterst C., Ghersi E., Baki L., Xu C., Serban G., et al. Metalloproteinase/Presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling. EMBO J 2006, 25:1242-1252.
    • (2006) EMBO J , vol.25 , pp. 1242-1252
    • Georgakopoulos, A.1    Litterst, C.2    Ghersi, E.3    Baki, L.4    Xu, C.5    Serban, G.6
  • 22
    • 0346363758 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate-induced release of the colony-stimulating factor 1 receptor cytoplasmic domain into the cytosol involves two separate cleavage events
    • Wilhelmsen K., van der Geer P. Phorbol 12-myristate 13-acetate-induced release of the colony-stimulating factor 1 receptor cytoplasmic domain into the cytosol involves two separate cleavage events. Mol Cell Biol 2004, 24:454-464.
    • (2004) Mol Cell Biol , vol.24 , pp. 454-464
    • Wilhelmsen, K.1    van der Geer, P.2
  • 23
    • 34249664257 scopus 로고    scopus 로고
    • The insulin-like growth factor 1 (IGF-1) receptor is a substrate for gamma-secretase-mediated intramembrane proteolysis
    • McElroy B., Powell J.C., McCarthy J.V. The insulin-like growth factor 1 (IGF-1) receptor is a substrate for gamma-secretase-mediated intramembrane proteolysis. Biochem Biophys Res Commun 2007, 358:1136-1141.
    • (2007) Biochem Biophys Res Commun , vol.358 , pp. 1136-1141
    • McElroy, B.1    Powell, J.C.2    McCarthy, J.V.3
  • 24
    • 34250874502 scopus 로고    scopus 로고
    • Generation of intracellular domain of insulin receptor tyrosine kinase by gamma-secretase
    • Kasuga K., Kaneko H., Nishizawa M., Onodera O., Ikeuchi T. Generation of intracellular domain of insulin receptor tyrosine kinase by gamma-secretase. Biochem Biophys Res Commun 2007, 360:90-96.
    • (2007) Biochem Biophys Res Commun , vol.360 , pp. 90-96
    • Kasuga, K.1    Kaneko, H.2    Nishizawa, M.3    Onodera, O.4    Ikeuchi, T.5
  • 25
    • 44249115334 scopus 로고    scopus 로고
    • Gamma-Secretase: a multifaceted regulator of angiogenesis
    • Boulton M.E., Cai J., Grant M.B. gamma-Secretase: a multifaceted regulator of angiogenesis. J Cell Mol Med 2008, 12:781-795.
    • (2008) J Cell Mol Med , vol.12 , pp. 781-795
    • Boulton, M.E.1    Cai, J.2    Grant, M.B.3
  • 26
    • 72449211223 scopus 로고    scopus 로고
    • The cytotoxicity of gamma-secretase inhibitor I to breast cancer cells is mediated by proteasome inhibition, not by gamma-secretase inhibition
    • Han J., Ma I., Hendzel M.J., Allalunis-Turner J. The cytotoxicity of gamma-secretase inhibitor I to breast cancer cells is mediated by proteasome inhibition, not by gamma-secretase inhibition. Breast Cancer Res 2009, 11:R57.
    • (2009) Breast Cancer Res , vol.11
    • Han, J.1    Ma, I.2    Hendzel, M.J.3    Allalunis-Turner, J.4
  • 27
    • 49849089713 scopus 로고    scopus 로고
    • Neuregulin-1/ErbB signaling serves distinct functions in myelination of the peripheral and central nervous system
    • Brinkmann B.G., Agarwal A., Sereda M.W., Garratt A.N., Muller T., Wende H., et al. Neuregulin-1/ErbB signaling serves distinct functions in myelination of the peripheral and central nervous system. Neuron 2008, 59:581-595.
    • (2008) Neuron , vol.59 , pp. 581-595
    • Brinkmann, B.G.1    Agarwal, A.2    Sereda, M.W.3    Garratt, A.N.4    Muller, T.5    Wende, H.6
  • 28
    • 0141839882 scopus 로고    scopus 로고
    • Rac-dependent trans-endocytosis of ephrinBs regulates Eph-ephrin contact repulsion
    • Marston D.J., Dickinson S., Nobes C.D. Rac-dependent trans-endocytosis of ephrinBs regulates Eph-ephrin contact repulsion. Nat Cell Biol 2003, 5:879-888.
    • (2003) Nat Cell Biol , vol.5 , pp. 879-888
    • Marston, D.J.1    Dickinson, S.2    Nobes, C.D.3
  • 29
    • 0035824391 scopus 로고    scopus 로고
    • Gamma-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • Ni C.Y., Murphy M.P., Golde T.E., Carpenter G. Gamma-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science 2001, 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
  • 30
    • 0034616385 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-converting enzyme is required for cleavage of erbB4/HER4
    • Rio C., Buxbaum J.D., Peschon J.J., Corfas G. Tumor necrosis factor-alpha-converting enzyme is required for cleavage of erbB4/HER4. J Biol Chem 2000, 275:10379-10387.
    • (2000) J Biol Chem , vol.275 , pp. 10379-10387
    • Rio, C.1    Buxbaum, J.D.2    Peschon, J.J.3    Corfas, G.4
  • 31
    • 0141755325 scopus 로고    scopus 로고
    • Ectodomain cleavage of ErbB-4: characterization of the cleavage site and m80 fragment
    • Cheng Q.C., Tikhomirov O., Zhou W., Carpenter G. Ectodomain cleavage of ErbB-4: characterization of the cleavage site and m80 fragment. J Biol Chem 2003, 278:38421-38427.
    • (2003) J Biol Chem , vol.278 , pp. 38421-38427
    • Cheng, Q.C.1    Tikhomirov, O.2    Zhou, W.3    Carpenter, G.4
  • 32
    • 65249090883 scopus 로고    scopus 로고
    • ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor alpha, L-selectin, and tumor necrosis factor alpha
    • Le Gall S.M., Bobe P., Reiss K., Horiuchi K., Niu X.D., Lundell D., et al. ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor alpha, L-selectin, and tumor necrosis factor alpha. Mol Biol Cell 2009, 20:1785-1794.
    • (2009) Mol Biol Cell , vol.20 , pp. 1785-1794
    • Le Gall, S.M.1    Bobe, P.2    Reiss, K.3    Horiuchi, K.4    Niu, X.D.5    Lundell, D.6
  • 33
    • 35848968668 scopus 로고    scopus 로고
    • ErbB4 isoforms selectively regulate growth factor induced Madin-Darby canine kidney cell tubulogenesis
    • Zeng F., Zhang M.Z., Singh A.B., Zent R., Harris R.C. ErbB4 isoforms selectively regulate growth factor induced Madin-Darby canine kidney cell tubulogenesis. Mol Biol Cell 2007, 18:4446-4456.
    • (2007) Mol Biol Cell , vol.18 , pp. 4446-4456
    • Zeng, F.1    Zhang, M.Z.2    Singh, A.B.3    Zent, R.4    Harris, R.C.5
  • 34
    • 70249096642 scopus 로고    scopus 로고
    • ErbB4 splice variants Cyt1 and Cyt2 differ by 16 amino acids and exert opposing effects on the mammary epithelium in vivo
    • Muraoka-Cook R.S., Sandahl M.A., Strunk K.E., Miraglia L.C., Husted C., Hunter D.M., et al. ErbB4 splice variants Cyt1 and Cyt2 differ by 16 amino acids and exert opposing effects on the mammary epithelium in vivo. Mol Cell Biol 2009, 29:4935-4948.
    • (2009) Mol Cell Biol , vol.29 , pp. 4935-4948
    • Muraoka-Cook, R.S.1    Sandahl, M.A.2    Strunk, K.E.3    Miraglia, L.C.4    Husted, C.5    Hunter, D.M.6
  • 35
    • 21244487829 scopus 로고    scopus 로고
    • Presenilin-dependent gamma-secretase processing regulates multiple ERBB4/HER4 activities
    • Vidal G.A., Naresh A., Marrero L., Jones F.E. Presenilin-dependent gamma-secretase processing regulates multiple ERBB4/HER4 activities. J Biol Chem 2005, 280:19777-19783.
    • (2005) J Biol Chem , vol.280 , pp. 19777-19783
    • Vidal, G.A.1    Naresh, A.2    Marrero, L.3    Jones, F.E.4
  • 36
    • 33748288086 scopus 로고    scopus 로고
    • The intracellular domain of ErbB4 induces differentiation of mammary epithelial cells
    • Muraoka-Cook R.S., Sandahl M., Husted C., Hunter D., Miraglia L., Feng S.M., et al. The intracellular domain of ErbB4 induces differentiation of mammary epithelial cells. Mol Biol Cell 2006, 17:4118-4129.
    • (2006) Mol Biol Cell , vol.17 , pp. 4118-4129
    • Muraoka-Cook, R.S.1    Sandahl, M.2    Husted, C.3    Hunter, D.4    Miraglia, L.5    Feng, S.M.6
  • 37
    • 70350444721 scopus 로고    scopus 로고
    • Peptide EphB2/CTF2 generated by the gamma-secretase processing of EphB2 receptor promotes tyrosine phosphorylation and cell surface localization of N-methyl-d-aspartate receptors
    • Xu J., Litterst C., Georgakopoulos A., Zaganas I., Robakis N.K. Peptide EphB2/CTF2 generated by the gamma-secretase processing of EphB2 receptor promotes tyrosine phosphorylation and cell surface localization of N-methyl-d-aspartate receptors. J Biol Chem 2009, 284:27220-27228.
    • (2009) J Biol Chem , vol.284 , pp. 27220-27228
    • Xu, J.1    Litterst, C.2    Georgakopoulos, A.3    Zaganas, I.4    Robakis, N.K.5
  • 38
    • 34447510955 scopus 로고    scopus 로고
    • Ligand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptor
    • Litterst C., Georgakopoulos A., Shioi J., Ghersi E., Wisniewski T., Wang R., et al. Ligand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptor. J Biol Chem 2007, 282:16155-16163.
    • (2007) J Biol Chem , vol.282 , pp. 16155-16163
    • Litterst, C.1    Georgakopoulos, A.2    Shioi, J.3    Ghersi, E.4    Wisniewski, T.5    Wang, R.6
  • 39
    • 79959217449 scopus 로고    scopus 로고
    • PEDF regulates vascular permeability by a gamma-secretase-mediated pathway
    • Cai J., Wu L., Qi X., Li Calzi S., Caballero S., Shaw L., et al. PEDF regulates vascular permeability by a gamma-secretase-mediated pathway. PLoS One 2011, 6:e21164.
    • (2011) PLoS One , vol.6
    • Cai, J.1    Wu, L.2    Qi, X.3    Li Calzi, S.4    Caballero, S.5    Shaw, L.6
  • 40
    • 33645635929 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor inhibits angiogenesis via regulated intracellular proteolysis of vascular endothelial growth factor receptor 1
    • Cai J., Jiang W.G., Grant M.B., Boulton M. Pigment epithelium-derived factor inhibits angiogenesis via regulated intracellular proteolysis of vascular endothelial growth factor receptor 1. J Biol Chem 2006, 281:3604-3613.
    • (2006) J Biol Chem , vol.281 , pp. 3604-3613
    • Cai, J.1    Jiang, W.G.2    Grant, M.B.3    Boulton, M.4
  • 41
    • 77955736995 scopus 로고    scopus 로고
    • Type 1 insulin-like growth factor receptor translocates to the nucleus of human tumor cells
    • Aleksic T., Chitnis M.M., Perestenko O.V., Gao S., Thomas P.H., Turner G.D., et al. Type 1 insulin-like growth factor receptor translocates to the nucleus of human tumor cells. Cancer Res 2010, 70:6412-6419.
    • (2010) Cancer Res , vol.70 , pp. 6412-6419
    • Aleksic, T.1    Chitnis, M.M.2    Perestenko, O.V.3    Gao, S.4    Thomas, P.H.5    Turner, G.D.6
  • 42
    • 77951628921 scopus 로고    scopus 로고
    • SUMOylation mediates the nuclear translocation and signaling of the IGF-1 receptor
    • Sehat B., Tofigh A., Lin Y., Trocme E., Liljedahl U., Lagergren J., et al. SUMOylation mediates the nuclear translocation and signaling of the IGF-1 receptor. Sci Signal 2010, 3:ra10.
    • (2010) Sci Signal , vol.3
    • Sehat, B.1    Tofigh, A.2    Lin, Y.3    Trocme, E.4    Liljedahl, U.5    Lagergren, J.6
  • 43
    • 78651364746 scopus 로고    scopus 로고
    • Over-accumulation of nuclear IGF-1 receptor in tumor cells requires elevated expression of the receptor and the SUMO-conjugating enzyme Ubc9
    • Deng H., Lin Y., Badin M., Vasilcanu D., Stromberg T., Jernberg-Wiklund H., et al. Over-accumulation of nuclear IGF-1 receptor in tumor cells requires elevated expression of the receptor and the SUMO-conjugating enzyme Ubc9. Biochem Biophys Res Commun 2011, 404:667-671.
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 667-671
    • Deng, H.1    Lin, Y.2    Badin, M.3    Vasilcanu, D.4    Stromberg, T.5    Jernberg-Wiklund, H.6
  • 44
    • 4644247974 scopus 로고    scopus 로고
    • Trafficking and signaling pathways of nuclear localizing protein ligands and their receptors
    • Johnson H.M., Subramaniam P.S., Olsnes S., Jans D.A. Trafficking and signaling pathways of nuclear localizing protein ligands and their receptors. Bioessays 2004, 26:993-1004.
    • (2004) Bioessays , vol.26 , pp. 993-1004
    • Johnson, H.M.1    Subramaniam, P.S.2    Olsnes, S.3    Jans, D.A.4
  • 45
    • 24944578655 scopus 로고    scopus 로고
    • Nuclear translocation of cell-surface receptors: lessons from fibroblast growth factor
    • Bryant D.M., Stow J.L. Nuclear translocation of cell-surface receptors: lessons from fibroblast growth factor. Traffic 2005, 6:947-954.
    • (2005) Traffic , vol.6 , pp. 947-954
    • Bryant, D.M.1    Stow, J.L.2
  • 46
    • 11144274556 scopus 로고    scopus 로고
    • Regulation of endocytosis, nuclear translocation, and signaling of fibroblast growth factor receptor 1 by E-cadherin
    • Bryant D.M., Wylie F.G., Stow J.L. Regulation of endocytosis, nuclear translocation, and signaling of fibroblast growth factor receptor 1 by E-cadherin. Mol Biol Cell 2005, 16:14-23.
    • (2005) Mol Biol Cell , vol.16 , pp. 14-23
    • Bryant, D.M.1    Wylie, F.G.2    Stow, J.L.3
  • 47
    • 28544448741 scopus 로고    scopus 로고
    • Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor
    • Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G., et al. Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor. Mol Cell Biol 2005, 25:11005-11018.
    • (2005) Mol Cell Biol , vol.25 , pp. 11005-11018
    • Giri, D.K.1    Ali-Seyed, M.2    Li, L.Y.3    Lee, D.F.4    Ling, P.5    Bartholomeusz, G.6
  • 48
    • 33746561717 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic transport of EGFR involves receptor endocytosis, importin beta1 and CRM1
    • Lo H.W., Ali-Seyed M., Wu Y., Bartholomeusz G., Hsu S.C., Hung M.C. Nuclear-cytoplasmic transport of EGFR involves receptor endocytosis, importin beta1 and CRM1. J Cell Biochem 2006, 98:1570-1583.
    • (2006) J Cell Biochem , vol.98 , pp. 1570-1583
    • Lo, H.W.1    Ali-Seyed, M.2    Wu, Y.3    Bartholomeusz, G.4    Hsu, S.C.5    Hung, M.C.6
  • 49
    • 0034041537 scopus 로고    scopus 로고
    • Nuclear targeting signal recognition: a key control point in nuclear transport?
    • Jans D.A., Xiao C.Y., Lam M.H. Nuclear targeting signal recognition: a key control point in nuclear transport?. Bioessays 2000, 22:532-544.
    • (2000) Bioessays , vol.22 , pp. 532-544
    • Jans, D.A.1    Xiao, C.Y.2    Lam, M.H.3
  • 50
    • 8644262258 scopus 로고    scopus 로고
    • Importin beta: conducting a much larger cellular symphony
    • Harel A., Forbes D.J. Importin beta: conducting a much larger cellular symphony. Mol Cell 2004, 16:319-330.
    • (2004) Mol Cell , vol.16 , pp. 319-330
    • Harel, A.1    Forbes, D.J.2
  • 51
    • 0037445982 scopus 로고    scopus 로고
    • Nuclear trafficking of FGFR1: a role for the transmembrane domain
    • Myers J.M., Martins G.G., Ostrowski J., Stachowiak M.K. Nuclear trafficking of FGFR1: a role for the transmembrane domain. J Cell Biochem 2003, 88:1273-1291.
    • (2003) J Cell Biochem , vol.88 , pp. 1273-1291
    • Myers, J.M.1    Martins, G.G.2    Ostrowski, J.3    Stachowiak, M.K.4
  • 52
    • 34249845380 scopus 로고    scopus 로고
    • Characterization of a novel tripartite nuclear localization sequence in the EGFR family
    • Hsu S.C., Hung M.C. Characterization of a novel tripartite nuclear localization sequence in the EGFR family. J Biol Chem 2007, 282:10432-10440.
    • (2007) J Biol Chem , vol.282 , pp. 10432-10440
    • Hsu, S.C.1    Hung, M.C.2
  • 53
    • 77249132723 scopus 로고    scopus 로고
    • Cyclooxygenase-2 is a novel transcriptional target of the nuclear EGFR-STAT3 and EGFRvIII-STAT3 signaling axes
    • Lo H.W., Cao X., Zhu H., Ali-Osman F. Cyclooxygenase-2 is a novel transcriptional target of the nuclear EGFR-STAT3 and EGFRvIII-STAT3 signaling axes. Mol Cancer Res 2010, 8:232-245.
    • (2010) Mol Cancer Res , vol.8 , pp. 232-245
    • Lo, H.W.1    Cao, X.2    Zhu, H.3    Ali-Osman, F.4
  • 54
    • 75749143418 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the early stage of protein translocation through the Sec translocon
    • Mori T., Ishitani R., Tsukazaki T., Nureki O., Sugita Y. Molecular mechanisms underlying the early stage of protein translocation through the Sec translocon. Biochemistry 2010, 49:945-950.
    • (2010) Biochemistry , vol.49 , pp. 945-950
    • Mori, T.1    Ishitani, R.2    Tsukazaki, T.3    Nureki, O.4    Sugita, Y.5
  • 55
    • 33947118714 scopus 로고    scopus 로고
    • Role of the Sec61 translocon in EGF receptor trafficking to the nucleus and gene expression
    • Liao H.J., Carpenter G. Role of the Sec61 translocon in EGF receptor trafficking to the nucleus and gene expression. Mol Biol Cell 2007, 18:1064-1072.
    • (2007) Mol Biol Cell , vol.18 , pp. 1064-1072
    • Liao, H.J.1    Carpenter, G.2
  • 56
    • 78649681031 scopus 로고    scopus 로고
    • The translocon Sec61beta localized in the inner nuclear membrane transports membrane-embedded EGF receptor to the nucleus
    • Wang Y.N., Yamaguchi H., Huo L., Du Y., Lee H.J., Lee H.H., et al. The translocon Sec61beta localized in the inner nuclear membrane transports membrane-embedded EGF receptor to the nucleus. J Biol Chem 2010, 285:38720-38729.
    • (2010) J Biol Chem , vol.285 , pp. 38720-38729
    • Wang, Y.N.1    Yamaguchi, H.2    Huo, L.3    Du, Y.4    Lee, H.J.5    Lee, H.H.6
  • 58
    • 57749196733 scopus 로고    scopus 로고
    • Tracing the retrograde route in protein trafficking
    • Johannes L., Popoff V. Tracing the retrograde route in protein trafficking. Cell 2008, 135:1175-1187.
    • (2008) Cell , vol.135 , pp. 1175-1187
    • Johannes, L.1    Popoff, V.2
  • 59
    • 0037010141 scopus 로고    scopus 로고
    • Transport of protein toxins into cells: pathways used by ricin, cholera toxin and Shiga toxin
    • Sandvig K., van Deurs B. Transport of protein toxins into cells: pathways used by ricin, cholera toxin and Shiga toxin. FEBS Lett 2002, 529:49-53.
    • (2002) FEBS Lett , vol.529 , pp. 49-53
    • Sandvig, K.1    van Deurs, B.2
  • 60
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • Hampton R.Y. ER-associated degradation in protein quality control and cellular regulation. Curr Opin Cell Biol 2002, 14:476-482.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 61
    • 77956265420 scopus 로고    scopus 로고
    • COPI-mediated retrograde trafficking from the Golgi to the ER regulates EGFR nuclear transport
    • Wang Y.N., Wang H., Yamaguchi H., Lee H.J., Lee H.H., Hung M.C. COPI-mediated retrograde trafficking from the Golgi to the ER regulates EGFR nuclear transport. Biochem Biophys Res Commun 2010, 399:498-504.
    • (2010) Biochem Biophys Res Commun , vol.399 , pp. 498-504
    • Wang, Y.N.1    Wang, H.2    Yamaguchi, H.3    Lee, H.J.4    Lee, H.H.5    Hung, M.C.6
  • 62
    • 40849124319 scopus 로고    scopus 로고
    • Membrane-anchored growth factor, HB-EGF, on the cell surface targeted to the inner nuclear membrane
    • Hieda M., Isokane M., Koizumi M., Higashi C., Tachibana T., Shudou M., et al. Membrane-anchored growth factor, HB-EGF, on the cell surface targeted to the inner nuclear membrane. J Cell Biol 2008, 180:763-769.
    • (2008) J Cell Biol , vol.180 , pp. 763-769
    • Hieda, M.1    Isokane, M.2    Koizumi, M.3    Higashi, C.4    Tachibana, T.5    Shudou, M.6
  • 63
    • 33749072714 scopus 로고    scopus 로고
    • Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain
    • Sardi S.P., Murtie J., Koirala S., Patten B.A., Corfas G. Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain. Cell 2006, 127:185-197.
    • (2006) Cell , vol.127 , pp. 185-197
    • Sardi, S.P.1    Murtie, J.2    Koirala, S.3    Patten, B.A.4    Corfas, G.5
  • 64
    • 8444243682 scopus 로고    scopus 로고
    • The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone
    • Williams C.C., Allison J.G., Vidal G.A., Burow M.E., Beckman B.S., Marrero L., et al. The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone. J Cell Biol 2004, 167:469-478.
    • (2004) J Cell Biol , vol.167 , pp. 469-478
    • Williams, C.C.1    Allison, J.G.2    Vidal, G.A.3    Burow, M.E.4    Beckman, B.S.5    Marrero, L.6
  • 65
    • 0242550638 scopus 로고    scopus 로고
    • Impaired differentiation and lactational failure of Erbb4-deficient mammary glands identify ERBB4 as an obligate mediator of STAT5
    • Long W., Wagner K.U., Lloyd K.C., Binart N., Shillingford J.M., Hennighausen L., et al. Impaired differentiation and lactational failure of Erbb4-deficient mammary glands identify ERBB4 as an obligate mediator of STAT5. Development 2003, 130:5257-5268.
    • (2003) Development , vol.130 , pp. 5257-5268
    • Long, W.1    Wagner, K.U.2    Lloyd, K.C.3    Binart, N.4    Shillingford, J.M.5    Hennighausen, L.6
  • 67
    • 33748087796 scopus 로고    scopus 로고
    • Coregulation of estrogen receptor by ERBB4/HER4 establishes a growth-promoting autocrine signal in breast tumor cells
    • Zhu Y., Sullivan L.L., Nair S.S., Williams C.C., Pandey A.K., Marrero L., et al. Coregulation of estrogen receptor by ERBB4/HER4 establishes a growth-promoting autocrine signal in breast tumor cells. Cancer Res 2006, 66:7991-7998.
    • (2006) Cancer Res , vol.66 , pp. 7991-7998
    • Zhu, Y.1    Sullivan, L.L.2    Nair, S.S.3    Williams, C.C.4    Pandey, A.K.5    Marrero, L.6
  • 68
    • 24744450988 scopus 로고    scopus 로고
    • Secretase-dependent tyrosine phosphorylation of Mdm2 by the ErbB-4 intracellular domain fragment
    • Arasada R.R., Carpenter G. Secretase-dependent tyrosine phosphorylation of Mdm2 by the ErbB-4 intracellular domain fragment. J Biol Chem 2005, 280:30783-30787.
    • (2005) J Biol Chem , vol.280 , pp. 30783-30787
    • Arasada, R.R.1    Carpenter, G.2
  • 69
    • 41949128060 scopus 로고    scopus 로고
    • Isoform-specific monoubiquitination, endocytosis, and degradation of alternatively spliced ErbB4 isoforms
    • Sundvall M., Korhonen A., Paatero I., Gaudio E., Melino G., Croce C.M., et al. Isoform-specific monoubiquitination, endocytosis, and degradation of alternatively spliced ErbB4 isoforms. Proc Natl Acad Sci U S A 2008, 105:4162-4167.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 4162-4167
    • Sundvall, M.1    Korhonen, A.2    Paatero, I.3    Gaudio, E.4    Melino, G.5    Croce, C.M.6
  • 70
    • 0034855942 scopus 로고    scopus 로고
    • Nuclear localization of EGF receptor and its potential new role as a transcription factor
    • Lin S.Y., Makino K., Xia W., Matin A., Wen Y., Kwong K.Y., et al. Nuclear localization of EGF receptor and its potential new role as a transcription factor. Nat Cell Biol 2001, 3:802-808.
    • (2001) Nat Cell Biol , vol.3 , pp. 802-808
    • Lin, S.Y.1    Makino, K.2    Xia, W.3    Matin, A.4    Wen, Y.5    Kwong, K.Y.6
  • 71
    • 35148832569 scopus 로고    scopus 로고
    • Epidermal growth factor receptor cooperates with signal transducer and activator of transcription 3 to induce epithelial-mesenchymal transition in cancer cells via up-regulation of TWIST gene expression
    • Lo H.W., Hsu S.C., Xia W., Cao X., Shih J.Y., Wei Y., et al. Epidermal growth factor receptor cooperates with signal transducer and activator of transcription 3 to induce epithelial-mesenchymal transition in cancer cells via up-regulation of TWIST gene expression. Cancer Res 2007, 67:9066-9076.
    • (2007) Cancer Res , vol.67 , pp. 9066-9076
    • Lo, H.W.1    Hsu, S.C.2    Xia, W.3    Cao, X.4    Shih, J.Y.5    Wei, Y.6
  • 72
    • 48349140762 scopus 로고    scopus 로고
    • Nuclear epidermal growth factor receptor (EGFR) interacts with signal transducer and activator of transcription 5 (STAT5) in activating Aurora-A gene expression
    • Hung L.Y., Tseng J.T., Lee Y.C., Xia W., Wang Y.N., Wu M.L., et al. Nuclear epidermal growth factor receptor (EGFR) interacts with signal transducer and activator of transcription 5 (STAT5) in activating Aurora-A gene expression. Nucleic Acids Res 2008, 36:4337-4351.
    • (2008) Nucleic Acids Res , vol.36 , pp. 4337-4351
    • Hung, L.Y.1    Tseng, J.T.2    Lee, Y.C.3    Xia, W.4    Wang, Y.N.5    Wu, M.L.6
  • 75
    • 4544376914 scopus 로고    scopus 로고
    • Binding at and transactivation of the COX-2 promoter by nuclear tyrosine kinase receptor ErbB-2
    • Wang S.C., Lien H.C., Xia W., Chen I.F., Lo H.W., Wang Z., et al. Binding at and transactivation of the COX-2 promoter by nuclear tyrosine kinase receptor ErbB-2. Cancer Cell 2004, 6:251-261.
    • (2004) Cancer Cell , vol.6 , pp. 251-261
    • Wang, S.C.1    Lien, H.C.2    Xia, W.3    Chen, I.F.4    Lo, H.W.5    Wang, Z.6
  • 76
    • 80052953818 scopus 로고    scopus 로고
    • Global identification of androgen response elements
    • Massie C.E., Mills I.G. Global identification of androgen response elements. Methods Mol Biol 2011, 776:255-273.
    • (2011) Methods Mol Biol , vol.776 , pp. 255-273
    • Massie, C.E.1    Mills, I.G.2
  • 77
    • 79960071366 scopus 로고    scopus 로고
    • The androgen receptor fuels prostate cancer by regulating central metabolism and biosynthesis
    • Massie C.E., Lynch A., Ramos-Montoya A., Boren J., Stark R., Fazli L., et al. The androgen receptor fuels prostate cancer by regulating central metabolism and biosynthesis. EMBO J 2011, 30:2719-2733.
    • (2011) EMBO J , vol.30 , pp. 2719-2733
    • Massie, C.E.1    Lynch, A.2    Ramos-Montoya, A.3    Boren, J.4    Stark, R.5    Fazli, L.6
  • 78
    • 33751508862 scopus 로고    scopus 로고
    • Tyrosine phosphorylation controls PCNA function through protein stability
    • Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C., et al. Tyrosine phosphorylation controls PCNA function through protein stability. Nat Cell Biol 2006, 8:1359-1368.
    • (2006) Nat Cell Biol , vol.8 , pp. 1359-1368
    • Wang, S.C.1    Nakajima, Y.2    Yu, Y.L.3    Xia, W.4    Chen, C.T.5    Yang, C.C.6
  • 79
    • 33644987412 scopus 로고    scopus 로고
    • Interaction of the epidermal growth factor receptor and the DNA-dependent protein kinase pathway following gefitinib treatment
    • Friedmann B.J., Caplin M., Savic B., Shah T., Lord C.J., Ashworth A., et al. Interaction of the epidermal growth factor receptor and the DNA-dependent protein kinase pathway following gefitinib treatment. Mol Cancer Ther 2006, 5:209-218.
    • (2006) Mol Cancer Ther , vol.5 , pp. 209-218
    • Friedmann, B.J.1    Caplin, M.2    Savic, B.3    Shah, T.4    Lord, C.J.5    Ashworth, A.6
  • 80
    • 11244280137 scopus 로고    scopus 로고
    • Novel prognostic value of nuclear epidermal growth factor receptor in breast cancer
    • Lo H.W., Xia W., Wei Y., Ali-Seyed M., Huang S.F., Hung M.C. Novel prognostic value of nuclear epidermal growth factor receptor in breast cancer. Cancer Res 2005, 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
  • 81
    • 75149186207 scopus 로고    scopus 로고
    • Increased expression of vascular endothelial growth factor-C and nuclear CXCR4 in hepatocellular carcinoma is correlated with lymph node metastasis and poor outcome
    • Xiang Z., Zeng Z., Tang Z., Fan J., Sun H., Wu W., et al. Increased expression of vascular endothelial growth factor-C and nuclear CXCR4 in hepatocellular carcinoma is correlated with lymph node metastasis and poor outcome. Cancer J 2009, 15:519-525.
    • (2009) Cancer J , vol.15 , pp. 519-525
    • Xiang, Z.1    Zeng, Z.2    Tang, Z.3    Fan, J.4    Sun, H.5    Wu, W.6
  • 82
    • 79959548959 scopus 로고    scopus 로고
    • Elevated BCRP/ABCG2 expression confers acquired resistance to gefitinib in wild-type EGFR-expressing cells
    • Chen Y.J., Huang W.C., Wei Y.L., Hsu S.C., Yuan P., Lin H.Y., et al. Elevated BCRP/ABCG2 expression confers acquired resistance to gefitinib in wild-type EGFR-expressing cells. PLoS One 2011, 6:e21428.
    • (2011) PLoS One , vol.6
    • Chen, Y.J.1    Huang, W.C.2    Wei, Y.L.3    Hsu, S.C.4    Yuan, P.5    Lin, H.Y.6
  • 83
    • 59049104003 scopus 로고    scopus 로고
    • Functions of the breast cancer resistance protein (BCRP/ABCG2) in chemotherapy
    • Noguchi K., Katayama K., Mitsuhashi J., Sugimoto Y. Functions of the breast cancer resistance protein (BCRP/ABCG2) in chemotherapy. Adv Drug Deliv Rev 2009, 61:26-33.
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 26-33
    • Noguchi, K.1    Katayama, K.2    Mitsuhashi, J.3    Sugimoto, Y.4
  • 84
    • 67649185566 scopus 로고    scopus 로고
    • Activated Akt prevents antitumor activity of gefitinib in renal cancer cells
    • Kuroda K., Horiguchi A., Sumitomo M., Asano T., Ito K., Hayakawa M. Activated Akt prevents antitumor activity of gefitinib in renal cancer cells. Urology 2009, 74:209-215.
    • (2009) Urology , vol.74 , pp. 209-215
    • Kuroda, K.1    Horiguchi, A.2    Sumitomo, M.3    Asano, T.4    Ito, K.5    Hayakawa, M.6
  • 85
    • 2342471392 scopus 로고    scopus 로고
    • Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib
    • Lynch T.J., Bell D.W., Sordella R., Gurubhagavatula S., Okimoto R.A., Brannigan B.W., et al. Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib. N Engl J Med 2004, 350:2129-2139.
    • (2004) N Engl J Med , vol.350 , pp. 2129-2139
    • Lynch, T.J.1    Bell, D.W.2    Sordella, R.3    Gurubhagavatula, S.4    Okimoto, R.A.5    Brannigan, B.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.