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Volumn 5, Issue 10, 2013, Pages

Receptor tyrosine kinases in the nucleus

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE FRAGMENT; PROTEIN TYROSINE KINASE; SECRETASE;

EID: 84885073436     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a008979     Document Type: Review
Times cited : (92)

References (172)
  • 1
    • 71049140394 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor maintains retinal pigment epithelium function by inhibiting vascular endothelial growth factor-R2 signaling through γ-secretase
    • Ablonczy Z, Prakasam A, Fant J, Fauq A, Crosson C, Sam-bamurti K. 2009. Pigment epithelium-derived factor maintains retinal pigment epithelium function by inhibiting vascular endothelial growth factor-R2 signaling through γ-secretase. J Biol Chem 284: 30177-30286.
    • (2009) J Biol Chem , vol.284 , pp. 30177-30286
    • Ablonczy, Z.1    Prakasam, A.2    Fant, J.3    Fauq, A.4    Crosson, C.5    Sambamurti, K.6
  • 2
    • 79955745746 scopus 로고    scopus 로고
    • A nuclear variant of ErbB3 receptor tyrosine kinase regulates ezrin distribution and Schwann cell mye-lination
    • Adilakshmi T, Ness-Myers J, Madrid-Aliste C, Fiser A, Tapi-nos N. 2011. A nuclear variant of ErbB3 receptor tyrosine kinase regulates ezrin distribution and Schwann cell mye-lination. J Neurosci 31: 5106-5119.
    • (2011) J Neurosci , vol.31 , pp. 5106-5119
    • Adilakshmi, T.1    Ness-Myers, J.2    Madrid-Aliste, C.3    Fiser, A.4    Tapi-Nos, N.5
  • 4
    • 79955664273 scopus 로고    scopus 로고
    • The ERBB4 intracellular domain (4ICD) regulates NRG1-in-duced gene expression in hippocampal neurons
    • Allison JG, Das PM, Ma J, Inglis FM, Jones FE. 2011. The ERBB4 intracellular domain (4ICD) regulates NRG1-in-duced gene expression in hippocampal neurons. Neurosci Res 70: 155-163.
    • (2011) Neurosci Res , vol.70 , pp. 155-163
    • Allison, J.G.1    Das, P.M.2    Ma, J.3    Inglis, F.M.4    Jones, F.E.5
  • 5
    • 67349106681 scopus 로고    scopus 로고
    • Proteolytic cleavages give receptor tyrosine kinases the gift of ubiquity
    • Ancot F, Foveau B, Lefebvre J, Leroy C, Tulasne D. 2009. Proteolytic cleavages give receptor tyrosine kinases the gift of ubiquity. Oncogene 28: 2185-2195.
    • (2009) Oncogene , vol.28 , pp. 2185-2195
    • Ancot, F.1    Foveau, B.2    Lefebvre, J.3    Leroy, C.4    Tulasne, D.5
  • 6
    • 84857122831 scopus 로고    scopus 로고
    • ErbB3(80 kDa), a nuclear variant of the ErbB3 receptor, binds to the Cyclin D1promoter to activate cell proliferation but is negatively controlled by p14ARF
    • Andrique L, Fauvin D, El Maassarani M, Colasson H, Van-nier B, Séité P. 2012. ErbB3(80 kDa), a nuclear variant of the ErbB3 receptor, binds to the Cyclin D1promoter to activate cell proliferation but is negatively controlled by p14ARF. Cell Signal 24: 1074-1085.
    • (2012) Cell Signal , vol.24 , pp. 1074-1085
    • Andrique, L.1    Fauvin, D.2    El Maassarani, M.3    Colasson, H.4    Van-Nier, B.5    Séité, P.6
  • 7
    • 33746290773 scopus 로고    scopus 로고
    • Biosynthesis of tumorigen-ic HER2 C-terminal fragments byalternative initiation of translation
    • Anido J, Scaltriti M, Bech Serra JJ, Santiago Josefat B, Todo FR, Baselga J, Arribas J. 2006. Biosynthesis of tumorigen-ic HER2 C-terminal fragments byalternative initiation of translation. EMBO J 25: 3234-3244.
    • (2006) EMBO J , vol.25 , pp. 3234-3244
    • Anido, J.1    Scaltriti, M.2    Bech, S.J.J.3    Santiago, J.B.4    Todo, F.R.5    Baselga, J.6    Arribas, J.7
  • 10
    • 84862003773 scopus 로고    scopus 로고
    • Cooperation of nuclear fibroblast growth factor receptor 1 and Nurr1 offers new interactive mechanism in postmitotic development of mesencephalic dopami-nergic neurons
    • Baron O, Förthmann B, Lee YW, Terranova C, Ratzka A, Stachowiak EK, Grothe C, Claus P, Stachowiak MK. 2012. Cooperation of nuclear fibroblast growth factor receptor 1 and Nurr1 offers new interactive mechanism in postmitotic development of mesencephalic dopami-nergic neurons. J Biol Chem 287: 19827-19840.
    • (2012) J Biol Chem , vol.287 , pp. 19827-19840
    • Baron, O.1    Förthmann, B.2    Lee, Y.W.3    Terranova, C.4    Ratzka, A.5    Stachowiak, E.K.6    Grothe, C.7    Claus, P.8    Stachowiak, M.K.9
  • 11
    • 78649740898 scopus 로고    scopus 로고
    • Progesterone receptor induces ErbB-2 nuclear translocation to promote breast cancer growth via a novel transcriptional effect: ErbB-2 function as a coactivator of Stat3
    • Béguelin W, Díaz FlaquéMC, Proietti CJ, Cayrol F, Rivas MA, Tkach M, Rosemblit C, Tocci JM, Charreau EH, et al. 2010. Progesterone receptor induces ErbB-2 nuclear translocation to promote breast cancer growth via a novel transcriptional effect: ErbB-2 function as a coactivator of Stat3. Mol Cell Biol 30: 5456-5472.
    • (2010) Mol Cell Biol , vol.30 , pp. 5456-5472
    • Béguelin, W.1    Díaz, F.M.C.2    Proietti, C.J.3    Cayrol, F.4    Rivas, M.A.5    Tkach, M.6    Rosemblit, C.7    Tocci, J.M.8    Charreau, E.H.9
  • 12
    • 16544391027 scopus 로고    scopus 로고
    • Caspase-8-dependent HER-2 cleavage in response to tumor necrosis factor a stimulation is counteracted by nuclear factor kB through c-FLIP-L expression
    • Benoit V, Chariot A, Delacroix L, Deregowski V, Jacobs N, Merville MP, Bours V. 2004. Caspase-8-dependent HER-2 cleavage in response to tumor necrosis factor a stimulation is counteracted by nuclear factor kB through c-FLIP-L expression. Cancer Res 64: 2684-2691.
    • (2004) Cancer Res , vol.64 , pp. 2684-2691
    • Benoit, V.1    Chariot, A.2    Delacroix, L.3    Deregowski, V.4    Jacobs, N.5    Merville, M.P.6    Bours, V.7
  • 13
    • 77952394976 scopus 로고    scopus 로고
    • MUC1 regulates nuclear localization and function of the epidermal growth factor receptor
    • Bitler BG, Goverdhan A, Schroeder JA. 2010. MUC1 regulates nuclear localization and function of the epidermal growth factor receptor. J Cell Sci 123: 1716-1723.
    • (2010) J Cell Sci , vol.123 , pp. 1716-1723
    • Bitler, B.G.1    Goverdhan, A.2    Schroeder, J.A.3
  • 15
    • 67349097494 scopus 로고    scopus 로고
    • Retrograde transport from endosomes to the trans-Golgi network
    • Bonifacino JS, Rojas R. 2006. Retrograde transport from endosomes to the trans-Golgi network. Nat Rev Cell Mol Biol 7: 563-579.
    • (2006) Nat Rev Cell Mol Biol , vol.7 , pp. 563-579
    • Bonifacino, J.S.1    Rojas, R.2
  • 17
    • 68549111215 scopus 로고    scopus 로고
    • Nuclear trafficking and functions of endocytic proteins implicated in oncogene-sis
    • Borlido J, Zecchini V, Mills IG. 2009. Nuclear trafficking and functions of endocytic proteins implicated in oncogene-sis. Traffic 10: 1209-1220.
    • (2009) Traffic , vol.10 , pp. 1209-1220
    • Borlido, J.1    Zecchini, V.2    Mills, I.G.3
  • 18
    • 33747623018 scopus 로고    scopus 로고
    • Notch signalling: A simple pathway becomes complex
    • Bray SJ. 2006. Notch signalling: A simple pathway becomes complex. Nat Rev Mol Cell Biol 7: 678-689.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 678-689
    • Bray, S.J.1
  • 19
    • 78049273362 scopus 로고    scopus 로고
    • Proteolytic processing of protocadherin proteins requires endocyto-sis
    • Buchanan SM, Schalm SS, Maniatis T. 2010. Proteolytic processing of protocadherin proteins requires endocyto-sis. Proc Natl Acad Sci 107: 17774-17779.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 17774-17779
    • Buchanan, S.M.1    Schalm, S.S.2    Maniatis, T.3
  • 21
  • 22
    • 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 WG, Grant MB, Boulton M. 2006. Pigment epithelium-derived factor inhibits angiogenesis via regulated intracellular proteolysis of vascular endothelial growth factor receptor 1. J Biol Chem 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
  • 25
    • 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
  • 26
    • 67349270856 scopus 로고    scopus 로고
    • Trafficking of receptor tyrosine kinases to the nucleus
    • Carpenter G, Liao HJ. 2009. Trafficking of receptor tyrosine kinases to the nucleus. Exp Cell Res 315: 1556-1566.
    • (2009) Exp Cell Res , vol.315 , pp. 1556-1566
    • Carpenter, G.1    Liao, H.J.2
  • 27
    • 48849100795 scopus 로고    scopus 로고
    • The cytoplasmic tail of MUC1: A very busy place
    • Carson DD. 2008. The cytoplasmic tail of MUC1: A very busy place. Sci Signal 1: e35.
    • (2008) Sci Signal , vol.1
    • Carson, D.D.1
  • 30
    • 77954367715 scopus 로고    scopus 로고
    • The p75NTR intracellular domain generated by neurotrophin-induced receptor cleavage potentiates Trk signaling
    • Ceni C, Kommaddi RP, Thomas R, Vereker E, Liu X, McPherson PS, Ritter B, Barker PA. 2010. The p75NTR intracellular domain generated by neurotrophin-induced receptor cleavage potentiates Trk signaling. J Cell Sci 123: 2299-22307.
    • (2010) J Cell Sci , vol.123 , pp. 2299-22307
    • Ceni, C.1    Kommaddi, R.P.2    Thomas, R.3    Vereker, E.4    Liu, X.5    McPherson, P.S.6    Ritter, B.7    Barker, P.A.8
  • 31
    • 0343397638 scopus 로고    scopus 로고
    • Up-regulation of nuclear IGF-I receptor by short term exposure of stilbene estrogen, di-ethylstilbestrol
    • Chen CW, Roy D. 1996. Up-regulation of nuclear IGF-I receptor by short term exposure of stilbene estrogen, di-ethylstilbestrol. Mol Cell Endocrinol 118: 1-8.
    • (1996) Mol Cell Endocrinol , vol.118 , pp. 1-8
    • Chen, C.W.1    Roy, D.2
  • 32
    • 0141755325 scopus 로고    scopus 로고
    • Ectodomain cleavage of ErbB-4: Characterization of the cleavage site and m80 fragment
    • Cheng QC, Tikhomirov O, Zhou W, Carpenter G. 2003. Ectodomain cleavage of ErbB-4: Characterization of the cleavage site and m80 fragment. J Biol Chem 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
  • 33
    • 84864001533 scopus 로고    scopus 로고
    • FGFR1 cleavage and nuclear translocation regulates breast cancer cell behavior
    • Chioni AM, Grose R. 2012. FGFR1 cleavage and nuclear translocation regulates breast cancer cell behavior. J Cell Biol 197: 801-817.
    • (2012) J Cell Biol , vol.197 , pp. 801-817
    • Chioni, A.M.1    Grose, R.2
  • 34
    • 0033559210 scopus 로고    scopus 로고
    • Cleavage of the HER2 ectodomain is a pervanadate-activable process that is inhibited by the tissue inhibitor of metalloproteases-1 in breast cancer cells
    • Codony-Servat J, Albanell J, Lopez-Talavera JC, Arribas J, Baselga J. 1999. Cleavage of the HER2 ectodomain is a pervanadate-activable process that is inhibited by the tissue inhibitor of metalloproteases-1 in breast cancer cells. Cancer Res 59: 1196-11201.
    • (1999) Cancer Res , vol.59 , pp. 1196-11201
    • Codony-Servat, J.1    Albanell, J.2    Lopez-Talavera, J.C.3    Arribas, J.4    Baselga, J.5
  • 35
    • 79751508853 scopus 로고    scopus 로고
    • Translocation of the cytoplasmic domain of ADAM13 to the nucleus is essential for Calpain8-a expression and cranial neural crest cell migration
    • Cousin H, Abbruzzese G, Kerdavid E, Gaultier A, Alfandari D. 2011. Translocation of the cytoplasmic domain of ADAM13 to the nucleus is essential for Calpain8-a expression and cranial neural crest cell migration. Dev Cell 20: 256-263.
    • (2011) Dev Cell , vol.20 , pp. 256-263
    • Cousin, H.1    Abbruzzese, G.2    Kerdavid, E.3    Gaultier, A.4    Alfandari, D.5
  • 37
    • 80054702141 scopus 로고    scopus 로고
    • Ligand activation leads to regulated intramembrane proteolysis of fibroblast growth factor receptor 3
    • Degnin CR, Laederich MB, Horton WA. 2011. Ligand activation leads to regulated intramembrane proteolysis of fibroblast growth factor receptor 3. Mol Biol Cell 22: 3861-3873.
    • (2011) Mol Biol Cell , vol.22 , pp. 3861-3873
    • Degnin, C.R.1    Laederich, M.B.2    Horton, W.A.3
  • 39
    • 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, Strömberg T, Jern-berg-Wiklund H, Sehat B, Larsson O. 2010. 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 404: 667-671.
    • (2010) Biochem Biophys Res Commun , vol.404 , pp. 667-671
    • Deng, H.1    Lin, Y.2    Badin, M.3    Vasilcanu, D.4    Strömberg, T.5    Jernberg-Wiklund, H.6    Sehat, B.7    Larsson, O.8
  • 41
    • 78049374467 scopus 로고    scopus 로고
    • Novel research horizons for presenilins and γ-secretases in cell biology and disease
    • De Strooper B, Annaert W. 2010. Novel research horizons for presenilins and γ-secretases in cell biology and disease. Annu Rev Cell Dev Biol 26: 235-260.
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 235-260
    • de Strooper, B.1    Annaert, W.2
  • 43
    • 77956939857 scopus 로고    scopus 로고
    • Nuclear EGFR shuttling induced by ionizing radiation is regulated by phosphor-ylation at residue Thr654
    • Dittmann K, Mayer C, Fehrenbacher B, Schaller M, Kehl-bach R, Rodemann HP. 2010. Nuclear EGFR shuttling induced by ionizing radiation is regulated by phosphor-ylation at residue Thr654. FEBS Lett 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
  • 46
    • 0030685131 scopus 로고    scopus 로고
    • A novel juxtamembrane domain iso-form of HER4/ErbB4. Isoform-specific tissue distribution and differential processing in response to phorbol ester
    • Elenius K, Corfas G, Paul S, Choi CJ, Rio C, Plowman GD, Klagsbrun M. 1997. A novel juxtamembrane domain iso-form of HER4/ErbB4. Isoform-specific tissue distribution and differential processing in response to phorbol ester. J Biol Chem 272: 26761-26768.
    • (1997) J Biol Chem , vol.272 , pp. 26761-26768
    • Elenius, K.1    Corfas, G.2    Paul, S.3    Choi, C.J.4    Rio, C.5    Plowman, G.D.6    Klagsbrun, M.7
  • 48
    • 65549121943 scopus 로고    scopus 로고
    • Notch signaling: The core pathway and its posttranslational regulation
    • Fortini ME. 2009. Notch signaling: The core pathway and its posttranslational regulation. Dev Cell 16: 633-647.
    • (2009) Dev Cell , vol.16 , pp. 633-647
    • Fortini, M.E.1
  • 49
    • 33947359937 scopus 로고    scopus 로고
    • Amplification of apoptosis through sequential caspase cleavage of the MET tyrosine kinase receptor
    • Foveau B, Leroy C, Ancot F, Deheuninck J, Ji Z, Fafeur V, Tulasne D. 2007. Amplification of apoptosis through sequential caspase cleavage of the MET tyrosine kinase receptor. Cell Death Differ 14: 752-764.
    • (2007) Cell Death Differ , vol.14 , pp. 752-764
    • Foveau, B.1    Leroy, C.2    Ancot, F.3    Deheuninck, J.4    Ji, Z.5    Fafeur, V.6    Tulasne, D.7
  • 51
    • 1542285106 scopus 로고    scopus 로고
    • Phosphorylated KDR is expressed in the neoplastic and stromal elements of human renal tumours and shuttles from cell membrane to nucleus
    • Fox SB, Turley H, Cheale M, Blázquez C, Roberts H, James N, Cook N, Harris A, Gatter K. 2004. Phosphorylated KDR is expressed in the neoplastic and stromal elements of human renal tumours and shuttles from cell membrane to nucleus. J Pathol 202: 313-320.
    • (2004) J Pathol , vol.202 , pp. 313-320
    • Fox, S.B.1    Turley, H.2    Cheale, M.3    Blázquez, C.4    Roberts, H.5    James, N.6    Cook, N.7    Harris, A.8    Gatter, K.9
  • 53
    • 80053931329 scopus 로고    scopus 로고
    • Presenilin1/γ-secretase promotes the EphB2-induced phosphorylation of ephrinB2 by regulating phosphoprotein associated with glycosphingolipid-enriched microdomains/Csk binding protein
    • Georgakopoulos A, Xu J, Xu C, Mauger G, Barthet G, Ro-bakis NK. 2011. Presenilin1/γ-secretase promotes the EphB2-induced phosphorylation of ephrinB2 by regulating phosphoprotein associated with glycosphingolipid-enriched microdomains/Csk binding protein. FASEB J 25: 3594-3604.
    • (2011) FASEB J , vol.25 , pp. 3594-3604
    • Georgakopoulos, A.1    Xu, J.2    Xu, C.3    Mauger, G.4    Barthet, G.5    Robakis, N.K.6
  • 56
    • 36049023803 scopus 로고    scopus 로고
    • CSF-1 and TPA stimulate independent pathways leading to lysosomal degradation or regulated intramembrane proteolysis of the CSF-1 receptor
    • Glenn G, van der Geer P. 2007. CSF-1 and TPA stimulate independent pathways leading to lysosomal degradation or regulated intramembrane proteolysis of the CSF-1 receptor. FEBS Lett 581: 5377-5381.
    • (2007) FEBS Lett , vol.581 , pp. 5377-5381
    • Glenn, G.1    van der Geer, P.2
  • 57
    • 40149107848 scopus 로고    scopus 로고
    • Toll-like receptors stimulate regulated intramembrane proteolysis of the CSF-1 receptor through Erk activation
    • Glenn G, van der Geer P. 2008. Toll-like receptors stimulate regulated intramembrane proteolysis of the CSF-1 receptor through Erk activation. FEBS Lett 582: 911-915.
    • (2008) FEBS Lett , vol.582 , pp. 911-915
    • Glenn, G.1    van der Geer, P.2
  • 58
    • 44949138816 scopus 로고    scopus 로고
    • The neogenin intracellular domain regulates gene transcription via nuclear translocation
    • Goldschneider D, Rama N, Guix C, Mehlen P. 2008. The neogenin intracellular domain regulates gene transcription via nuclear translocation. Mol Cell Biol 28: 4068-4079.
    • (2008) Mol Cell Biol , vol.28 , pp. 4068-4079
    • Goldschneider, D.1    Rama, N.2    Guix, C.3    Mehlen, P.4
  • 59
    • 84871343626 scopus 로고    scopus 로고
    • Insights into ectodomain shedding and processing of protein-tyrosine pseudoki-nase 7 (PTK7)
    • Golubkov VS, Strongin AY. 2012. Insights into ectodomain shedding and processing of protein-tyrosine pseudoki-nase 7 (PTK7). J Biol Chem 287: 42009-42018.
    • (2012) J Biol Chem , vol.287 , pp. 42009-42018
    • Golubkov, V.S.1    Strongin, A.Y.2
  • 62
    • 79954623907 scopus 로고    scopus 로고
    • Characterization and comparison of protein complexes initiated by the intracellular domain of individual Notch paralogs
    • Han J, Allalunis-Turner J, Hendzel MJ. 2011. Characterization and comparison of protein complexes initiated by the intracellular domain of individual Notch paralogs. Biochem Biophys Res Commun 407: 479-485.
    • (2011) Biochem Biophys Res Commun , vol.407 , pp. 479-485
    • Han, J.1    Allalunis-Turner, J.2    Hendzel, M.J.3
  • 66
    • 34249845380 scopus 로고    scopus 로고
    • Characterization of a novel tripartite nuclear localization sequence in the EGFR family
    • Hsu SC, Hung MC. 2007. Characterization of a novel tripartite nuclear localization sequence in the EGFR family. J Biol Chem 282: 10432-10440.
    • (2007) J Biol Chem , vol.282 , pp. 10432-10440
    • Hsu, S.C.1    Hung, M.C.2
  • 67
    • 79957982003 scopus 로고    scopus 로고
    • Nuclear translocationof epidermal growth factor receptorbyAkt-dependent phosphorylation enhances breast cancer-resistant protein expression in gefitinib-resistant cells
    • Huang WC, Chen YJ, Li LY, Wei YL, Hsu SC, Tsai SL, Chiu PC, Huang WP, Wang YN, Chen CH, etal. 2011a. Nuclear translocationof epidermal growth factor receptorbyAkt-dependent phosphorylation enhances breast cancer-resistant protein expression in gefitinib-resistant cells. J Biol Chem 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    Chiu, P.C.7    Huang, W.P.8    Wang, Y.N.9    Chen, C.H.10
  • 68
    • 80053038156 scopus 로고    scopus 로고
    • Epithelial cell adhesion molecule (EpCAM) complex proteins promote transcription factor-mediated pluripo-tency reprogramming
    • Huang HP, Chen PH, Yu CY, Chuang CY, Stone L, Hsiao WC, Li CL, Tsai SC, Chen KY, Chen HF, et al. 2011b. Epithelial cell adhesion molecule (EpCAM) complex proteins promote transcription factor-mediated pluripo-tency reprogramming. J Biol Chem 286: 33520-33532.
    • (2011) J Biol Chem , vol.286 , pp. 33520-33532
    • Huang, H.P.1    Chen, P.H.2    Yu, C.Y.3    Chuang, C.Y.4    Stone, L.5    Hsiao, W.C.6    Li, C.L.7    Tsai, S.C.8    Chen, K.Y.9    Chen, H.F.10
  • 70
    • 44149120446 scopus 로고    scopus 로고
    • HER4 intracellular domain (4ICD) activity in the developing mammary gland and breast cancer
    • Jones FE. 2008. HER4 intracellular domain (4ICD) activity in the developing mammary gland and breast cancer. J Mammary Gland Biol Neoplasia 13: 247-258.
    • (2008) J Mammary Gland Biol Neoplasia , vol.13 , pp. 247-258
    • Jones, F.E.1
  • 71
    • 79954989679 scopus 로고    scopus 로고
    • A novel signaling pathway mediated by the nuclear targeting of C-terminal fragments of mammalian Patched 1
    • Kagawa H, Shino Y, Kobayashi D, Demizu S, Shimada M, Ariga H, Kawahara H. 2011. A novel signaling pathway mediated by the nuclear targeting of C-terminal fragments of mammalian Patched 1. PLoS ONE 6: e18638.
    • (2011) PLoS ONE , vol.6
    • Kagawa, H.1    Shino, Y.2    Kobayashi, D.3    Demizu, S.4    Shimada, M.5    Ariga, H.6    Kawahara, H.7
  • 72
  • 74
    • 2942557122 scopus 로고    scopus 로고
    • G-Secretase: Proteasome of the membrane?
    • Kopan R, Ilagan MX. 2004. G-Secretase: Proteasome of the membrane? Nat Rev Mol Cell Biol 5: 499-504.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 75
    • 0346374724 scopus 로고    scopus 로고
    • Implication of γ-secretase in neuregu-lin-induced maturation of ligodendrocytes
    • Lai C, Feng L. 2004. Implication of γ-secretase in neuregu-lin-induced maturation of ligodendrocytes. Biochem Bio-phys Res Commun 314: 535-542.
    • (2004) Biochem Bio-phys Res Commun , vol.314 , pp. 535-542
    • Lai, C.1    Feng, L.2
  • 76
    • 79955061701 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: Signaling pathways and biological functions
    • Lal M, Caplan M. 2011. Regulated intramembrane proteolysis: Signaling pathways and biological functions. Physiology (Bethesda) 26: 34-44.
    • (2011) Physiology (Bethesda) , vol.26 , pp. 34-44
    • Lal, M.1    Caplan, M.2
  • 77
    • 34347205690 scopus 로고    scopus 로고
    • Vascular endothelial growth factor mediates intracrine survival in human breast carcinoma cells through internally expressed VEGFR1/FLT1
    • Lee TH, Seng S, Sekine M, Hinton C, Fu Y, Avraham HK, Avraham S. 2007. Vascular endothelial growth factor mediates intracrine survival in human breast carcinoma cells through internally expressed VEGFR1/FLT1. PLoS Med 4: e186.
    • (2007) PLoS Med , vol.4
    • Lee, T.H.1    Seng, S.2    Sekine, M.3    Hinton, C.4    Fu, Y.5    Avraham, H.K.6    Avraham, S.7
  • 78
    • 80051669175 scopus 로고    scopus 로고
    • Intramembrane proteolysis in regulated protein trafficking
    • Lemberg MK. 2011. Intramembrane proteolysis in regulated protein trafficking. Traffic 12: 1109-1118.
    • (2011) Traffic , vol.12 , pp. 1109-1118
    • Lemberg, M.K.1
  • 79
    • 80555135912 scopus 로고    scopus 로고
    • Oxygen-dependent cleavage of the p75 neurotrophin receptor triggers stabilization of HIF-1a
    • Le Moan N, Houslay DM, Christian F, Houslay MD, Akas-soglou K. 2011. Oxygen-dependent cleavage of the p75 neurotrophin receptor triggers stabilization of HIF-1a. Mol Cell 44: 476-490.
    • (2011) Mol Cell , vol.44 , pp. 476-490
    • Le Moan, N.1    Houslay, D.M.2    Christian, F.3    Houslay, M.D.4    Akas-Soglou, K.5
  • 81
    • 33947118714 scopus 로고    scopus 로고
    • Role of the Sec61 translocon in EGF receptor trafficking to the nucleus and gene expression
    • Liao HJ, Carpenter G. 2007. Role of the Sec61 translocon in EGF receptor trafficking to the nucleus and gene expression. Mol Biol Cell 18: 1064-1072.
    • (2007) Mol Biol Cell , vol.18 , pp. 1064-1072
    • Liao, H.J.1    Carpenter, G.2
  • 82
    • 68049129871 scopus 로고    scopus 로고
    • Cetuximab/C225-induced in-tracellular trafficking of epidermal growth factor receptor
    • Liao HJ, Carpenter G. 2009. Cetuximab/C225-induced in-tracellular trafficking of epidermal growth factor receptor. Cancer Res 69: 6179-6183.
    • (2009) Cancer Res , vol.69 , pp. 6179-6183
    • Liao, H.J.1    Carpenter, G.2
  • 83
    • 84863868124 scopus 로고    scopus 로고
    • Regulated intramembrane cleavage of the EGF receptor
    • Liao HJ, Carpenter G. 2012. Regulated intramembrane cleavage of the EGF receptor. Traffic 13: 1106-1112.
    • (2012) Traffic , vol.13 , pp. 1106-1112
    • Liao, H.J.1    Carpenter, G.2
  • 84
    • 79551510855 scopus 로고    scopus 로고
    • EGFR nuclear translocation modulates DNA repair following cisplatin and ionizing radiation treatment
    • Liccardi G, Hartley JA, Hochhauser D. 2011. EGFR nuclear translocation modulates DNA repair following cisplatin and ionizing radiation treatment. Cancer Res 71: 1103- 1114.
    • (2011) Cancer Res , vol.71 , pp. 1103-1114
    • Liccardi, G.1    Hartley, J.A.2    Hochhauser, D.3
  • 86
    • 57649221000 scopus 로고    scopus 로고
    • Ephrin-B2-induced cleavage of EphB2 receptor is mediated by matrix metalloproteinases to trigger cell repulsion
    • Lin KT, Sloniowski S, Ethell DW, Ethell IM. 2008. Ephrin-B2-induced cleavage of EphB2 receptor is mediated by matrix metalloproteinases to trigger cell repulsion. J Biol Chem 283: 28969-28979.
    • (2008) J Biol Chem , vol.283 , pp. 28969-28979
    • Lin, K.T.1    Sloniowski, S.2    Ethell, D.W.3    Ethell, I.M.4
  • 88
    • 77955408349 scopus 로고    scopus 로고
    • An unusual function of RON receptor tyrosine kinase as a transcrip-tional regulator in cooperation with EGFR in human cancer cells
    • Liu HS, Hsu PY, Lai MD, Chang HY, Ho CL, Cheng HL, Chen HT, Lin YJ, Wu TJ, Tzai TS, et al. 2010. An unusual function of RON receptor tyrosine kinase as a transcrip-tional regulator in cooperation with EGFR in human cancer cells. Carcinogenesis 31: 1456-1464.
    • (2010) Carcinogenesis , vol.31 , pp. 1456-1464
    • Liu, H.S.1    Hsu, P.Y.2    Lai, M.D.3    Chang, H.Y.4    Ho, C.L.5    Cheng, H.L.6    Chen, H.T.7    Lin, Y.J.8    Wu, T.J.9    Tzai, T.S.10
  • 90
    • 33746561717 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic transport of EGFR involves receptor endocytosis, importin b1 and CRM1
    • Lo HW, Ali-Seyed M, Wu Y, Bartholomeusz G, Hsu SC, Hung MC. 2006. Nuclear-cytoplasmic transport of EGFR involves receptor endocytosis, importin b1 and CRM1. J Cell Biochem 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
  • 91
    • 77249132723 scopus 로고    scopus 로고
    • Cyclooxygenase-2 is a novel transcriptional target of the nuclear EGFR-STA3 and EGFRvIII-STAT3 signaling axes
    • Lo HW, Cao X, Zhu H, Ali-Osman F. 2010. Cyclooxygenase-2 is a novel transcriptional target of the nuclear EGFR-STA3 and EGFRvIII-STAT3 signaling axes. Mol Cancer Res 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
  • 92
    • 77950012622 scopus 로고    scopus 로고
    • The regulatory crosstalk between kinases and proteases in cancer
    • López-Otín C, Hunter T. 2010. The regulatory crosstalk between kinases and proteases in cancer. Nat RevCancer 10: 278-292.
    • (2010) Nat RevCancer , vol.10 , pp. 278-292
    • López-Otín, C.1    Hunter, T.2
  • 93
    • 49049096654 scopus 로고    scopus 로고
    • Genetic mosaic analysis reveals FGF receptor 2 function in terminal end buds during mammary gland branching morphogenesis
    • Lu P, Ewald AJ, Martin GR, Werb Z. 2004. Genetic mosaic analysis reveals FGF receptor 2 function in terminal end buds during mammary gland branching morphogenesis. Dev Biol 321: 77-87.
    • (2004) Dev Biol , vol.321 , pp. 77-87
    • Lu, P.1    Ewald, A.J.2    Martin, G.R.3    Werb, Z.4
  • 94
    • 55349114398 scopus 로고    scopus 로고
    • Cleavage of the Wnt receptor Ryk regulates neuronal differentiation during cortical neurogenesis
    • Lyu J, Yamamoto V, Lu W. 2008. Cleavage of the Wnt receptor Ryk regulates neuronal differentiation during cortical neurogenesis. Dev Cell 15: 773-780.
    • (2008) Dev Cell , vol.15 , pp. 773-780
    • Lyu, J.1    Yamamoto, V.2    Lu, W.3
  • 95
    • 67649718401 scopus 로고    scopus 로고
    • Cdc37 regulates Ryk signaling by stabilizing the cleaved Ryk intracellular domain
    • Lyu J, Wesselschmidt RL, Lu W. 2009. Cdc37 regulates Ryk signaling by stabilizing the cleaved Ryk intracellular domain. J Biol Chem 284: 12940-12948.
    • (2009) J Biol Chem , vol.284 , pp. 12940-12948
    • Lyu, J.1    Wesselschmidt, R.L.2    Lu, W.3
  • 97
    • 35648952161 scopus 로고    scopus 로고
    • Regulated proteolytic processing of Tie1 modulates ligand responsiveness of the receptor-ty-rosine kinase Tie2
    • Marron MB, Singh H, Tahir TA, Kavumkal J, Kim HZ, Koh GY, Brindle NP. 2007. Regulated proteolytic processing of Tie1 modulates ligand responsiveness of the receptor-ty-rosine kinase Tie2. J Biol Chem 282: 30509-30517.
    • (2007) J Biol Chem , vol.282 , pp. 30509-30517
    • Marron, M.B.1    Singh, H.2    Tahir, T.A.3    Kavumkal, J.4    Kim, H.Z.5    Koh, G.Y.6    Brindle, N.P.7
  • 99
    • 28144441697 scopus 로고    scopus 로고
    • Wingless signaling at synapses isthrough cleavage and nuclear import of receptor DFrizzled2
    • Mathew D, Ataman B, Chen J, Zhang Y, Cumberledge S, Budnik V. 2005. Wingless signaling at synapses isthrough cleavage and nuclear import of receptor DFrizzled2. Science 310: 1344-1347.
    • (2005) Science , vol.310 , pp. 1344-1347
    • Mathew, D.1    Ataman, B.2    Chen, J.3    Zhang, Y.4    Cumberledge, S.5    Budnik, V.6
  • 101
    • 67649534694 scopus 로고    scopus 로고
    • Presenilin-depen-dent regulated intramembrane proteolysis and γ-secre-tase activity
    • McCarthy JV, Twomey C, Wujek P. 2009. Presenilin-depen-dent regulated intramembrane proteolysis and γ-secre-tase activity. Cell Mol Life Sci 66: 1534-1555.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1534-1555
    • McCarthy, J.V.1    Twomey, C.2    Wujek, P.3
  • 102
    • 34249664257 scopus 로고    scopus 로고
    • The insulin-like growth factor 1 (IGF-1) receptor is a substrate for γ-sec-retase-mediated intramembrane proteolysis
    • McElroy B, Powell JC, McCarthy JV. 2007. The insulin-like growth factor 1 (IGF-1) receptor is a substrate for γ-sec-retase-mediated intramembrane proteolysis. Biochem Bi-ophys Res Commun 358: 1136-1141.
    • (2007) Biochem Bi-ophys Res Commun , vol.358 , pp. 1136-1141
    • McElroy, B.1    Powell, J.C.2    McCarthy, J.V.3
  • 103
    • 79957895865 scopus 로고    scopus 로고
    • Galectin-3 regulates MUC1 and EGFR cellular distribution and EGFR downstream pathways in pancreatic cancer cells
    • Merlin J, Stechly L, de BeaucéS, Monté D, Leteurtre E, van Seuningen I, Huet G, Pigny P. 2011. Galectin-3 regulates MUC1 and EGFR cellular distribution and EGFR downstream pathways in pancreatic cancer cells. Oncogene 30: 2514-2525.
    • (2011) Oncogene , vol.30 , pp. 2514-2525
    • Merlin, J.1    Stechly, L.2    De BeaucéS3    Monté, D.4    Leteurtre, E.5    van Seuningen, I.6    Huet, G.7    Pigny, P.8
  • 104
    • 0029097546 scopus 로고
    • Mutational analysis of the membrane-proximal cleavage site of l-selectin: Relaxed sequence specificity surrounding the cleavage site
    • Migaki GI, Kahn J, Kishimoto TK. 1995. Mutational analysis of the membrane-proximal cleavage site of l-selectin: Relaxed sequence specificity surrounding the cleavage site. J Exp Med 182: 549-557.
    • (1995) J Exp Med , vol.182 , pp. 549-557
    • Migaki, G.I.1    Kahn, J.2    Kishimoto, T.K.3
  • 105
    • 84861732970 scopus 로고    scopus 로고
    • Identification of function for CD44 intracytoplasmic domain (CD44-ICD): Modulation of matrix metalloproteinase 9 (MMP-9) transcription via novel promoter response element
    • Miletti-González KE, Murphy K, Kumaran MN, Ravindra-nath AK, Wernyj RP, Kaur S, Miles GD, Lim E, Chan R, Chekmareva M, et al. 2012. Identification of function for CD44 intracytoplasmic domain (CD44-ICD): Modulation of matrix metalloproteinase 9 (MMP-9) transcription via novel promoter response element. J Biol Chem 287: 18995-19007.
    • (2012) J Biol Chem , vol.287 , pp. 18995-19007
    • Miletti-González, K.E.1    Murphy, K.2    Kumaran, M.N.3    Ravindra-Nath, A.K.4    Wernyj, R.P.5    Kaur, S.6    Miles, G.D.7    Lim, E.8    Chan, R.9    Chekmareva, M.10
  • 106
    • 77954615439 scopus 로고    scopus 로고
    • Ectodomain shedding of interleukin-2 receptor b and generation of an intracellular functional fragment
    • Montes de Oca P, Malardé V, Proust R, Dautry-Varsat A, Gesbert F. 2010. Ectodomain shedding of interleukin-2 receptor b and generation of an intracellular functional fragment. J Biol Chem 285: 22050-22058.
    • (2010) J Biol Chem , vol.285 , pp. 22050-22058
    • de Oca, M.P.1    Malardé, V.2    Proust, R.3    Dautry-Varsat, A.4    Gesbert, F.5
  • 110
    • 84864106172 scopus 로고    scopus 로고
    • The cytosolic domain of protein-tyrosine kinase 7 (PTK7), generated from sequential cleavagebya disintegrin and metallopro-tease 17 (ADAM17) and γ-secretase, enhances cell proliferation and migration in colon cancer cells
    • Na HW, Shin WS, Ludwig A, Lee ST. 2012. The cytosolic domain of protein-tyrosine kinase 7 (PTK7), generated from sequential cleavagebya disintegrin and metallopro-tease 17 (ADAM17) and γ-secretase, enhances cell proliferation and migration in colon cancer cells. J Biol Chem 287: 25001-25009.
    • (2012) J Biol Chem , vol.287 , pp. 25001-25009
    • Na, H.W.1    Shin, W.S.2    Ludwig, A.3    Lee, S.T.4
  • 112
    • 0035824391 scopus 로고    scopus 로고
    • G-Secre-tase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • Ni CY, Murphy MP, Golde TE, Carpenter G. 2001. G-Secre-tase 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
  • 113
    • 0003356476 scopus 로고    scopus 로고
    • Role of the ErbB-4 carboxyl terminus in γ-secretase cleavage
    • Ni CY, Yuan H, Carpenter G. 2003. Role of the ErbB-4 carboxyl terminus in γ-secretase cleavage. J Biol Chem 278: 4561-4565.
    • (2003) J Biol Chem , vol.278 , pp. 4561-4565
    • Ni, C.Y.1    Yuan, H.2    Carpenter, G.3
  • 117
    • 79956029624 scopus 로고    scopus 로고
    • Antipsychotic treatment and neuregulin 1-ErbB4 signalling in schizophrenia
    • Pan B, Huang XF, Deng C. 2011. Antipsychotic treatment and neuregulin 1-ErbB4 signalling in schizophrenia. Prog Neuropsychopharmacol Biol Psychiatry 35: 924-930.
    • (2011) Prog Neuropsychopharmacol Biol Psychiatry , vol.35 , pp. 924-930
    • Pan, B.1    Huang, X.F.2    Deng, C.3
  • 118
    • 77949322236 scopus 로고    scopus 로고
    • Nuclear localization of the p75 neurotrophin receptor intracellular domain
    • Parkhurst CN, Zampieri N, Chao MV. 2010. Nuclear localization of the p75 neurotrophin receptor intracellular domain. J Biol Chem 285: 5361-5368.
    • (2010) J Biol Chem , vol.285 , pp. 5361-5368
    • Parkhurst, C.N.1    Zampieri, N.2    Chao, M.V.3
  • 120
    • 84862308505 scopus 로고    scopus 로고
    • A novel epidermal growth factor receptor variant lacking multiple domains directly activates transcription and is overex-pressed in tumors
    • Piccione EC, Lieu TJ, Gentile CF, Williams TR, Connolly AJ, Godwin AK, Koong AC, Wong AJ. 2012. A novel epidermal growth factor receptor variant lacking multiple domains directly activates transcription and is overex-pressed in tumors. Oncogene 31: 2953-2967.
    • (2012) Oncogene , vol.31 , pp. 2953-2967
    • Piccione, E.C.1    Lieu, T.J.2    Gentile, C.F.3    Williams, T.R.4    Connolly, A.J.5    Godwin, A.K.6    Koong, A.C.7    Wong, A.J.8
  • 121
    • 33748076105 scopus 로고    scopus 로고
    • Met, the he-patocyte growth factor receptor, localizes to the nucleus in cells at low density
    • Pozner-Moulis S, Pappas DJ, Rimm DL. 2006. Met, the he-patocyte growth factor receptor, localizes to the nucleus in cells at low density. Cancer Res 66: 7976-7982.
    • (2006) Cancer Res , vol.66 , pp. 7976-7982
    • Pozner-Moulis, S.1    Pappas, D.J.2    Rimm, D.L.3
  • 122
    • 33746947883 scopus 로고    scopus 로고
    • Anaplastic lymphoma kinase is a dependence receptor whose proapoptotic functions are ctivated by caspase cleavage
    • Racaud-Sultan C, Gonzalez-Dunia D, Vigny M, Mehlen P, Delsol G, Allouche M. 2006. Anaplastic lymphoma kinase is a dependence receptor whose proapoptotic functions are ctivated by caspase cleavage. Mol Cell Biol 26: 6209-6222.
    • (2006) Mol Cell Biol , vol.26 , pp. 6209-6222
    • Racaud-Sultan, C.1    Gonzalez-Dunia, D.2    Vigny, M.3    Mehlen, P.4    Delsol, G.5    Allouche, M.6
  • 123
    • 65549153701 scopus 로고    scopus 로고
    • Identification of ligand-induced proteolytic cleavage and ectodomain shedding of VEGFR-1/FLT1 in leukemic cancer cells
    • Rahimi N, Golde TE, Meyer RD. 2009. Identification of ligand-induced proteolytic cleavage and ectodomain shedding of VEGFR-1/FLT1 in leukemic cancer cells. Cancer Res 69: 2607-2614.
    • (2009) Cancer Res , vol.69 , pp. 2607-2614
    • Rahimi, N.1    Golde, T.E.2    Meyer, R.D.3
  • 125
    • 70349332646 scopus 로고    scopus 로고
    • Nontraditional signaling mechanisms of lipoprotein receptors
    • Rebeck GW. 2009. Nontraditional signaling mechanisms of lipoprotein receptors. Sci Signal 2: e28.
    • (2009) Sci Signal , vol.2
    • Rebeck, G.W.1
  • 126
    • 0034616385 scopus 로고    scopus 로고
    • Tumor necrosis factor-a-converting enzyme is required for cleavage oferbB4/HER4
    • Rio C, Buxbaum JD, Peschon JJ, Corfas G. 2000. Tumor necrosis factor-a-converting enzyme is required for cleavage oferbB4/HER4.J Biol Chem 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
  • 127
    • 77953435123 scopus 로고    scopus 로고
    • The ERa coactivator, HER4/4ICD, regulates progesterone receptor expression in normal and malignant breast epithelium
    • Rokicki J, Das PM, Giltnane JM, Wansbury O, Rimm DL, Howard BA, Jones FE. 2010. The ERa coactivator, HER4/4ICD, regulates progesterone receptor expression in normal and malignant breast epithelium. Mol Cancer 9: 150.
    • (2010) Mol Cancer , vol.9 , pp. 150
    • Rokicki, J.1    Das, P.M.2    Giltnane, J.M.3    Wansbury, O.4    Rimm, D.L.5    Howard, B.A.6    Jones, F.E.7
  • 128
    • 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. 2002. Transport of protein toxins into cells: Pathways used by ricin, cholera toxin and Shiga toxin. FEBS Lett 529: 49-53.
    • (2002) FEBS Lett , vol.529 , pp. 49-53
    • Sandvig, K.1    van Deurs, B.2
  • 129
    • 2342486598 scopus 로고    scopus 로고
    • Internal and external autocrine VEGF/KDR loops regulate survival of subsets of acute leukemia through distinct signaling pathways
    • Santos SC, Dias S. 2004. Internal and external autocrine VEGF/KDR loops regulate survival of subsets of acute leukemia through distinct signaling pathways. Blood 103: 3883-3889.
    • (2004) Blood , vol.103 , pp. 3883-3889
    • Santos, S.C.1    Dias, S.2
  • 130
    • 34247102347 scopus 로고    scopus 로고
    • VEGF and VEGFR-2 (KDR) internalization is required for endothelial recovery during wound healing
    • Santos SC, Miguel C, Domingues I, Calado A, Zhu Z, Wu Y, Dias S. 2007. VEGF and VEGFR-2 (KDR) internalization is required for endothelial recovery during wound healing. Exp Cell Res 313: 1561-1574.
    • (2007) Exp Cell Res , vol.313 , pp. 1561-1574
    • Santos, S.C.1    Miguel, C.2    Domingues, I.3    Calado, A.4    Zhu, Z.5    Wu, Y.6    Dias, S.7
  • 131
    • 33749072714 scopus 로고    scopus 로고
    • Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain
    • Sardi SP, Murtie J, Koirala S, Patten BA, Corfas G. 2006. Presenilin-dependent ErbB4 nuclear signaling regulates the timing of astrogenesis in the developing brain. Cell 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
  • 132
    • 4444294105 scopus 로고    scopus 로고
    • Fgf9 induces proliferation and nuclear localization of FGFR2 in Sertoli precursors during male sex determination
    • Schmahl J, Kim Y, Colvin JS, Ornitz DM, Capel B.2004. Fgf9 induces proliferation and nuclear localization of FGFR2 in Sertoli precursors during male sex determination. Development 131: 3627-3636.
    • (2004) Development , vol.131 , pp. 3627-3636
    • Schmahl, J.1    Kim, Y.2    Colvin, J.S.3    Ornitz, D.M.4    Capel, B.5
  • 134
    • 35348860241 scopus 로고    scopus 로고
    • Presenilin: Running with scissors in the membrane
    • Selkoe DJ, Wolfe MS. 2007. Presenilin: Running with scissors in the membrane. Cell 131: 215-221.
    • (2007) Cell , vol.131 , pp. 215-221
    • Selkoe, D.J.1    Wolfe, M.S.2
  • 136
    • 0035997235 scopus 로고    scopus 로고
    • Is γ-secretase a multienzyme complex for membrane protein degradation? Models and speculations
    • Small DH. 2002. Is γ-secretase a multienzyme complex for membrane protein degradation? Models and speculations. Peptides 23: 1317-1321.
    • (2002) Peptides , vol.23 , pp. 1317-1321
    • Small, D.H.1
  • 137
    • 37249065138 scopus 로고    scopus 로고
    • Integra-tive nuclear signaling in cell development-A role for FGF receptor-1
    • Stachowiak MK, Maher PA, Stachowiak EK. 2007. Integra-tive nuclear signaling in cell development-A role for FGF receptor-1. DNA Cell Biol 26: 811-826.
    • (2007) DNA Cell Biol , vol.26 , pp. 811-826
    • Stachowiak, M.K.1    Maher, P.A.2    Stachowiak, E.K.3
  • 138
    • 10744227994 scopus 로고    scopus 로고
    • The angiogenic receptor KDR is widely distributed in human tissues and tumours and relocates intracellularly on phosphorylation. An immunohistochemical study
    • Stewart M, Turley H, Cook N, Pezzella F, Pillai G, Ogilvie D, Cartlidge S, Paterson D, Copley C, Kendrew J, et al. 2003. The angiogenic receptor KDR is widely distributed in human tissues and tumours and relocates intracellularly on phosphorylation. An immunohistochemical study. Histopathology 43: 33-39.
    • (2003) Histopathology , vol.43 , pp. 33-39
    • Stewart, M.1    Turley, H.2    Cook, N.3    Pezzella, F.4    Pillai, G.5    Ogilvie, D.6    Cartlidge, S.7    Paterson, D.8    Copley, C.9    Kendrew, J.10
  • 139
    • 77954380513 scopus 로고    scopus 로고
    • Sequential and γ-secretase-dependent processing of the β-cellulin precursor generates a palmitoylated intracellular-domain fragment that inhibits cell growth
    • Stoeck A, Shang L, Dempsey PJ. 2010. Sequential and γ-secretase-dependent processing of the β-cellulin precursor generates a palmitoylated intracellular-domain fragment that inhibits cell growth. J Cell Sci 123: 2319-2331.
    • (2010) J Cell Sci , vol.123 , pp. 2319-2331
    • Stoeck, A.1    Shang, L.2    Dempsey, P.J.3
  • 140
    • 49649107527 scopus 로고    scopus 로고
    • Caspase cleavage of HER-2 releases a bad-like cell death effector
    • Strohecker AM, Yehiely F, Chen F, Cryns VL. 2008. Caspase cleavage of HER-2 releases a bad-like cell death effector. J Biol Chem 283: 18269-18282.
    • (2008) J Biol Chem , vol.283 , pp. 18269-18282
    • Strohecker, A.M.1    Yehiely, F.2    Chen, F.3    Cryns, V.L.4
  • 141
    • 0033639117 scopus 로고    scopus 로고
    • Requirements for presenilin-de-pendent cleavage of notch and other transmembrane proteins
    • Struhl G, Adachi A. 2000. Requirements for presenilin-de-pendent cleavage of notch and other transmembrane proteins. Mol Cell 6: 625-636.
    • (2000) Mol Cell , vol.6 , pp. 625-636
    • Struhl, G.1    Adachi, A.2
  • 143
    • 19944433410 scopus 로고    scopus 로고
    • 1/S stage by Epstein-Barr-encoded oncoprotein latent membrane protein 1
    • Tao Y, Song X, Deng X, Xie D, Lee LM, Liu Y, Li W, Li L, Deng L, Wu Q, et al. 2005. Nuclear accumulation of epidermal growth factor receptor and acceleration of G1/S stage by Epstein-Barr-encoded oncoprotein latent membrane protein 1. Exp Cell Res 303: 240-251.
    • (2005) Exp Cell Res , vol.303 , pp. 240-251
    • Tao, Y.1    Song, X.2    Deng, X.3    Xie, D.4    Lee, L.M.5    Liu, Y.6    Li, W.7    Li, L.8    Deng, L.9    Wu, Q.10
  • 145
    • 73649135726 scopus 로고    scopus 로고
    • Subcellular localization of the HER4 ntracellular domain, 4ICD, identifies distinct prognostic outcomes for breast cancer patients
    • Thor AD, Edgerton SM, Jones FE. 2009. Subcellular localization of the HER4 ntracellular domain, 4ICD, identifies distinct prognostic outcomes for breast cancer patients. Am J Pathol 175: 1802-1809.
    • (2009) Am J Pathol , vol.175 , pp. 1802-1809
    • Thor, A.D.1    Edgerton, S.M.2    Jones, F.E.3
  • 146
    • 0035823554 scopus 로고    scopus 로고
    • Caspase-dependent cleavage of ErbB-2 by geldanamycin and staurosporin
    • Tikhomirov O, Carpenter G. 2001. Caspase-dependent cleavage of ErbB-2 by geldanamycin and staurosporin. J Biol Chem 276: 33675-33680.
    • (2001) J Biol Chem , vol.276 , pp. 33675-33680
    • Tikhomirov, O.1    Carpenter, G.2
  • 148
    • 66449103810 scopus 로고    scopus 로고
    • ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the γ-secretase
    • Tousseyn T, Thathiah A, Jorissen E, Raemaekers T, Ko-nietzko U, Reiss K, Maes E, Snellinx A, Serneels L, Nyabi O, et al. 2009. ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the γ-secretase. J Biol Chem 284: 11738-11747.
    • (2009) J Biol Chem , vol.284 , pp. 11738-11747
    • Tousseyn, T.1    Thathiah, A.2    Jorissen, E.3    Raemaekers, T.4    Ko-Nietzko, U.5    Reiss, K.6    Maes, E.7    Snellinx, A.8    Serneels, L.9    Nyabi, O.10
  • 150
    • 0030632048 scopus 로고    scopus 로고
    • The N-end rule pathway of protein degradation
    • Varshavsky A. 1997. The N-end rule pathway of protein degradation. Genes Cells 2: 13-28.
    • (1997) Genes Cells , vol.2 , pp. 13-28
    • Varshavsky, A.1
  • 151
    • 0029764504 scopus 로고    scopus 로고
    • Selective cleavage of the heregulin receptor ErbB-4 by protein kinase C activation
    • Vecchi M, Baulida J, Carpenter G. 1996. Selective cleavage of the heregulin receptor ErbB-4 by protein kinase C activation. J Biol Chem 271: 18989-18995.
    • (1996) J Biol Chem , vol.271 , pp. 18989-18995
    • Vecchi, M.1    Baulida, J.2    Carpenter, G.3
  • 153
    • 21244487829 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase processing regulates multiple ERBB4/HER4 activities
    • Vidal GA, Naresh A, Marrero L, Jones FE. 2005. Presenilin-dependent γ-secretase processing regulates multiple ERBB4/HER4 activities. J Biol Chem 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
  • 156
    • 78650170988 scopus 로고    scopus 로고
    • Inhibition of neurotrophin receptor p75 intramembran proteolysis by γ-secretase inhibitor reduces medulloblastoma spinal metastasis
    • Wang X, Cui M, Wang L, Chen X, Xin P. 2010a. Inhibition of neurotrophin receptor p75 intramembran proteolysis by γ-secretase inhibitor reduces medulloblastoma spinal metastasis. Biochem Biophys Res Commun 403: 264-269.
    • (2010) Biochem Biophys Res Commun , vol.403 , pp. 264-269
    • Wang, X.1    Cui, M.2    Wang, L.3    Chen, X.4    Xin, P.5
  • 157
    • 78649681031 scopus 로고    scopus 로고
    • The translocon Sec61b localized in the inner nuclear membrane transports membrane-embedded EGF receptor to the nucleus
    • Wang YN, Yamaguchi H, Huo L, Du Y, Lee HJ, Lee HH, Wang H, Hsu JM, Hung MC. 2010b. The translocon Sec61b localized in the inner nuclear membrane transports membrane-embedded EGF receptor to the nucleus. J Biol Chem 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    Wang, H.7    Hsu, J.M.8    Hung, M.C.9
  • 158
    • 77954759289 scopus 로고    scopus 로고
    • Nuclear trafficking of the epidermal growth factor receptor family membrane proteins
    • Wang YN, Yamaguchi H, Hsu JM, Hung MC. 2010c. Nuclear trafficking of the epidermal growth factor receptor family membrane proteins. Oncogene 29: 3997-4006.
    • (2010) Oncogene , vol.29 , pp. 3997-4006
    • Wang, Y.N.1    Yamaguchi, H.2    Hsu, J.M.3    Hung, M.C.4
  • 160
    • 77956265420 scopus 로고    scopus 로고
    • COPI-mediated retrograde trafficking from the Golgi to the ER regulates EGFR nuclear transport
    • Wang YN, Wang H, Yamaguchi H, Lee HJ, Lee HH, Hung MC. 2011b. COPI-mediated retrograde trafficking from the Golgi to the ER regulates EGFR nuclear transport. Biochem Biophys Res Commun 399: 498-504.
    • (2011) 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
  • 161
    • 84860872206 scopus 로고    scopus 로고
    • Membrane-bound trafficking regulates nuclear transport of integral epidermal growth factor receptor (EGFR) and ErbB-2
    • Wang YN, Lee HH, Lee HJ, Du Y, Yamaguchi H, Hung MC. 2012. Membrane-bound trafficking regulates nuclear transport of integral epidermal growth factor receptor (EGFR) and ErbB-2. J Biol Chem 287: 16869-16879.
    • (2012) J Biol Chem , vol.287 , pp. 16869-16879
    • Wang, Y.N.1    Lee, H.H.2    Lee, H.J.3    Du, Y.4    Yamaguchi, H.5    Hung, M.C.6
  • 162
    • 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. 2004. 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 24: 454-464.
    • (2004) Mol Cell Biol , vol.24 , pp. 454-464
    • Wilhelmsen, K.1    van der Geer, P.2
  • 163
    • 8444243682 scopus 로고    scopus 로고
    • The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone
    • Williams CC, Allison JG, Vidal GA, Burow ME, Beckman BS, Marrero L, Jones FE. 2004. The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone. J Cell Biol 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    Jones, F.E.7
  • 164
    • 67650550795 scopus 로고    scopus 로고
    • Transcriptional interaction of an estrogen receptor splice variant and ErbB4 suggests convergence in gene susceptibility pathways in schizophrenia
    • Wong J, Weickert CS. 2009. Transcriptional interaction of an estrogen receptor splice variant and ErbB4 suggests convergence in gene susceptibility pathways in schizophrenia. J Biol Chem 284: 18824-18832.
    • (2009) J Biol Chem , vol.284 , pp. 18824-18832
    • Wong, J.1    Weickert, C.S.2
  • 165
    • 80051589897 scopus 로고    scopus 로고
    • Truncated ErbB2 expressed in tumor cell nuclei contributes to acquired therapeutic resistance to ErbB2 kinase inhibitors
    • Xia W, Liu Z, Zong R, Liu L, Zhao S, Bacus SS, Mao Y, He J, Wulfkuhle JD, Petricoin EF III, et al. 2011. Truncated ErbB2 expressed in tumor cell nuclei contributes to acquired therapeutic resistance to ErbB2 kinase inhibitors. Mol Cancer Ther 10: 1367-1374.
    • (2011) Mol Cancer Ther , vol.10 , pp. 1367-1374
    • Xia, W.1    Liu, Z.2    Zong, R.3    Liu, L.4    Zhao, S.5    Bacus, S.S.6    Mao, Y.7    He, J.8    Wulfkuhle, J.D.9    Petricoin, E.F.10
  • 166
    • 84866128097 scopus 로고    scopus 로고
    • Nuclear EGFR suppresses ribonuclease activity of poly-nucleotide phosphorylase through DNAPK-mediated phosphorylation at serine 776
    • Yu YL, Chou RH, Wu CH, Wang YN, Chang WJ, Tseng YJ, Chang WC, Lai CC, Lee HJ, Huo L, et al. 2012. Nuclear EGFR suppresses ribonuclease activity of poly-nucleotide phosphorylase through DNAPK-mediated phosphorylation at serine 776. J Biol Chem 287: 31015-31026.
    • (2012) J Biol Chem , vol.287 , pp. 31015-31026
    • Yu, Y.L.1    Chou, R.H.2    Wu, C.H.3    Wang, Y.N.4    Chang, W.J.5    Tseng, Y.J.6    Chang, W.C.7    Lai, C.C.8    Lee, H.J.9    Huo, L.10
  • 167
    • 35848968668 scopus 로고    scopus 로고
    • ErbB4 isoforms selectively regulate growth factor induced Madin-Darby canine kidney cell tubulogenesis
    • Zeng F, Zhang MZ, Singh AB, Zent R, Harris RC. 2007. ErbB4 isoforms selectively regulate growth factor induced Madin-Darby canine kidney cell tubulogenesis. Mol Biol Cell 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
  • 168
    • 67649311930 scopus 로고    scopus 로고
    • Nedd4 mediates ErbB4 JM-a/ CYT-1 ICD ubiquitination and degradation in MDCK II cells
    • Zeng F, Xu J, Harris RC. 2009. Nedd4 mediates ErbB4 JM-a/ CYT-1 ICD ubiquitination and degradation in MDCK II cells. FASEB J 23: 1935-1945.
    • (2009) FASEB J , vol.23 , pp. 1935-1945
    • Zeng, F.1    Xu, J.2    Harris, R.C.3
  • 169
    • 23444458909 scopus 로고    scopus 로고
    • Expression and cellular localization of vascular endothelial growth factor A and its receptors in acute and chronic leukemias: An immunohistochem-ical study
    • Zhang Y, Pillai G, Gatter K, Blázquez C, Turley H, Pezzella F, Watt SM. 2005. Expression and cellular localization of vascular endothelial growth factor A and its receptors in acute and chronic leukemias: An immunohistochem-ical study. Hum Pathol 36: 797-805.
    • (2005) Hum Pathol , vol.36 , pp. 797-805
    • Zhang, Y.1    Pillai, G.2    Gatter, K.3    Blázquez, C.4    Turley, H.5    Pezzella, F.6    Watt, S.M.7
  • 170
    • 0034602333 scopus 로고    scopus 로고
    • Heregulin-dependent trafficking and cleavage of ErbB-4
    • Zhou W, Carpenter G. 2000. Heregulin-dependent trafficking and cleavage of ErbB-4. J Biol Chem 275: 34737-34743.
    • (2000) J Biol Chem , vol.275 , pp. 34737-34743
    • Zhou, W.1    Carpenter, G.2
  • 171
    • 80053633156 scopus 로고    scopus 로고
    • Neuregulin receptor ErbB4 functions as a transcriptional cofactor for the expression of surfactant protein B in the fetal lung
    • Zscheppang K, Dörk T, Schmiedl A, Jones FE, Dammann CE. 2011a. Neuregulin receptor ErbB4 functions as a transcriptional cofactor for the expression of surfactant protein B in the fetal lung. Am J Respir Cell Mol Biol 45: 761-767.
    • (2011) Am J Respir Cell Mol Biol , vol.45 , pp. 761-767
    • Zscheppang, K.1    Dörk, T.2    Schmiedl, A.3    Jones, F.E.4    Dammann, C.E.5
  • 172
    • 80051798255 scopus 로고    scopus 로고
    • Estrogen-induced upregulation of Sftpb requires transcriptional control of neuregulin receptor ErbB4 in mouse lung type II epithelial cells
    • Zscheppang K, Konrad M, Zischka M, Huhn V, Dammann CE. 2011b. Estrogen-induced upregulation of Sftpb requires transcriptional control of neuregulin receptor ErbB4 in mouse lung type II epithelial cells. Biochim Biophys Acta 1813: 1717-1727.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1717-1727
    • Zscheppang, K.1    Konrad, M.2    Zischka, M.3    Huhn, V.4    Dammann, C.E.5


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