메뉴 건너뛰기




Volumn 350, Issue 3, 2006, Pages 629-633

ErbB-4 and TNF-α converting enzyme localization to membrane microdomains

Author keywords

ErbB 4; Lipid rafts; Membrane microdomains; Receptor tyrosine kinase; Tumor necrosis factor converting enzyme

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 4; NEU DIFFERENTIATION FACTOR; POLYOXYETHYLENE OLEYL ETHER; TRITON X 100; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME;

EID: 33749665410     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.09.095     Document Type: Article
Times cited : (18)

References (30)
  • 2
    • 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., and Carpenter G. gamma-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science 294 (2001) 2179-2181
    • (2001) Science , vol.294 , pp. 2179-2181
    • Ni, C.Y.1    Murphy, M.P.2    Golde, T.E.3    Carpenter, G.4
  • 3
    • 0034602333 scopus 로고    scopus 로고
    • Heregulin-dependent trafficking and cleavage of ErbB-4
    • Zhou W., and Carpenter G. Heregulin-dependent trafficking and cleavage of ErbB-4. J. Biol. Chem. 275 (2000) 34737-34743
    • (2000) J. Biol. Chem. , vol.275 , pp. 34737-34743
    • Zhou, W.1    Carpenter, G.2
  • 4
    • 0029764504 scopus 로고    scopus 로고
    • Selective cleavage of the heregulin receptor ErbB-4 by protein kinase C activation
    • Vecchi M., Baulida J., and Carpenter G. Selective cleavage of the heregulin receptor ErbB-4 by protein kinase C activation. J. Biol. Chem. 271 (1996) 18989-18995
    • (1996) J. Biol. Chem. , vol.271 , pp. 18989-18995
    • Vecchi, M.1    Baulida, J.2    Carpenter, G.3
  • 5
    • 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., and Carpenter G. Ectodomain cleavage of ErbB-4: characterization of the cleavage site and m80 fragment. J. Biol. Chem. 278 (2003) 38421-38427
    • (2003) J. Biol. Chem. , vol.278 , pp. 38421-38427
    • Cheng, Q.C.1    Tikhomirov, O.2    Zhou, W.3    Carpenter, G.4
  • 6
    • 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., and Corfas G. Tumor necrosis factor-alpha-converting enzyme is required for cleavage of erbB4/HER4. J. Biol. Chem. 275 (2000) 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
  • 7
    • 0032493646 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and proteolysis. Pervanadate-induced, metalloprotease-dependent cleavage of the ErbB-4 receptor and amphiregulin
    • Vecchi M., Rudolph-Owen L.A., Brown C.L., Dempsey P.J., and Carpenter G. Tyrosine phosphorylation and proteolysis. Pervanadate-induced, metalloprotease-dependent cleavage of the ErbB-4 receptor and amphiregulin. J. Biol. Chem. 273 (1998) 20589-20595
    • (1998) J. Biol. Chem. , vol.273 , pp. 20589-20595
    • Vecchi, M.1    Rudolph-Owen, L.A.2    Brown, C.L.3    Dempsey, P.J.4    Carpenter, G.5
  • 9
    • 24744450988 scopus 로고    scopus 로고
    • Secretase-dependent tyrosine phosphorylation of Mdm2 by the ErbB-4 intracellular domain fragment
    • Arasada R.R., and Carpenter G. Secretase-dependent tyrosine phosphorylation of Mdm2 by the ErbB-4 intracellular domain fragment. J. Biol. Chem. 280 (2005) 30783-30787
    • (2005) J. Biol. Chem. , vol.280 , pp. 30783-30787
    • Arasada, R.R.1    Carpenter, G.2
  • 10
    • 23044492008 scopus 로고    scopus 로고
    • WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function
    • Aqeilan R.I., Donati V., Palamarchuk A., Trapasso F., Kaou M., Pekarsky Y., Sudol M., and Croce C.M. WW domain-containing proteins, WWOX and YAP, compete for interaction with ErbB-4 and modulate its transcriptional function. Cancer Res. 65 (2005) 6764-6772
    • (2005) Cancer Res. , vol.65 , pp. 6764-6772
    • Aqeilan, R.I.1    Donati, V.2    Palamarchuk, A.3    Trapasso, F.4    Kaou, M.5    Pekarsky, Y.6    Sudol, M.7    Croce, C.M.8
  • 13
    • 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., and Jones F.E. The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone. J. Cell Biol. 167 (2004) 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
  • 14
    • 1542358888 scopus 로고    scopus 로고
    • Ligand-regulated association of ErbB-4 to the transcriptional co-activator YAP65 controls transcription at the nuclear level
    • Omerovic J., Puggioni E.M., Napoletano S., Visco V., Fraioli R., Frati L., Gulino A., and Alimandi M. Ligand-regulated association of ErbB-4 to the transcriptional co-activator YAP65 controls transcription at the nuclear level. Exp. Cell Res. 294 (2004) 469-479
    • (2004) Exp. Cell Res. , vol.294 , pp. 469-479
    • Omerovic, J.1    Puggioni, E.M.2    Napoletano, S.3    Visco, V.4    Fraioli, R.5    Frati, L.6    Gulino, A.7    Alimandi, M.8
  • 15
    • 0042858208 scopus 로고    scopus 로고
    • WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus
    • Komuro A., Nagai M., Navin N.E., and Sudol M. WW domain-containing protein YAP associates with ErbB-4 and acts as a co-transcriptional activator for the carboxyl-terminal fragment of ErbB-4 that translocates to the nucleus. J. Biol. Chem. 278 (2003) 33334-33341
    • (2003) J. Biol. Chem. , vol.278 , pp. 33334-33341
    • Komuro, A.1    Nagai, M.2    Navin, N.E.3    Sudol, M.4
  • 16
    • 33748757331 scopus 로고    scopus 로고
    • ERBB-4 s80 intracellular domain abrogates ETO2-dependent transcriptional repression
    • Linggi B., and Carpenter G. ERBB-4 s80 intracellular domain abrogates ETO2-dependent transcriptional repression. J. Biol. Chem. (2006)
    • (2006) J. Biol. Chem.
    • Linggi, B.1    Carpenter, G.2
  • 17
    • 0034654554 scopus 로고    scopus 로고
    • Nuclear expression of the c-erbB-4/HER-4 growth factor receptor in invasive breast cancers
    • Srinivasan R., Gillett C.E., Barnes D.M., and Gullick W.J. Nuclear expression of the c-erbB-4/HER-4 growth factor receptor in invasive breast cancers. Cancer Res. 60 (2000) 1483-1487
    • (2000) Cancer Res. , vol.60 , pp. 1483-1487
    • Srinivasan, R.1    Gillett, C.E.2    Barnes, D.M.3    Gullick, W.J.4
  • 21
    • 30044432092 scopus 로고    scopus 로고
    • Proteolytic cleavage and phosphorylation of a tumor-associated ErbB4 isoform promote ligand-independent survival and cancer cell growth
    • Maatta J.A., Sundvall M., Junttila T.T., Peri L., Laine V.J.O., Isola J., Egeblad M., and Elenius K. Proteolytic cleavage and phosphorylation of a tumor-associated ErbB4 isoform promote ligand-independent survival and cancer cell growth. Mol. Biol. Cell 17 (2006) 67-79
    • (2006) Mol. Biol. Cell , vol.17 , pp. 67-79
    • Maatta, J.A.1    Sundvall, M.2    Junttila, T.T.3    Peri, L.4    Laine, V.J.O.5    Isola, J.6    Egeblad, M.7    Elenius, K.8
  • 22
    • 33748311706 scopus 로고    scopus 로고
    • A constitutively active ERBB4/HER4 allele with enhanced transcriptional coactivation and cell-killing activities
    • Vidal G.A., Clark D.E., Marrero L., and Jones F.E. A constitutively active ERBB4/HER4 allele with enhanced transcriptional coactivation and cell-killing activities. Oncogene (2006)
    • (2006) Oncogene
    • Vidal, G.A.1    Clark, D.E.2    Marrero, L.3    Jones, F.E.4
  • 25
    • 0028820041 scopus 로고
    • A detergent-free method for purifying caveolae membrane from tissue culture cells
    • Smart E.J., Ying Y.S., Mineo C., and Anderson R.G. A detergent-free method for purifying caveolae membrane from tissue culture cells. Proc. Natl. Acad. Sci. USA 92 (1995) 10104-10108
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10104-10108
    • Smart, E.J.1    Ying, Y.S.2    Mineo, C.3    Anderson, R.G.4
  • 26
    • 0030685131 scopus 로고    scopus 로고
    • A novel juxtamembrane domain isoform of HER4/ErbB4. Isoform-specific tissue distribution and differential processing in response to phorbol ester
    • Elenius K., Corfas G., Paul S., Choi C.J., Rio C., Plowman G.D., and Klagsbrun M. A novel juxtamembrane domain isoform of HER4/ErbB4. Isoform-specific tissue distribution and differential processing in response to phorbol ester. J. Biol. Chem. 272 (1997) 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
  • 27
    • 0038541768 scopus 로고    scopus 로고
    • Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE)
    • Schlondorff J., Becherer J.D., and Blobel C.P. Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE). Biochem. J. 34 Pt1 (2000) 131-138
    • (2000) Biochem. J. , vol.34 , Issue.Pt1 , pp. 131-138
    • Schlondorff, J.1    Becherer, J.D.2    Blobel, C.P.3
  • 28
    • 22844445240 scopus 로고    scopus 로고
    • Epidermal growth factor receptors are localized to lipid rafts that contain a balance of inner and outer leaflet lipids: a shotgun lipidomics study
    • Pike L.J., Han X., and Gross R.W. Epidermal growth factor receptors are localized to lipid rafts that contain a balance of inner and outer leaflet lipids: a shotgun lipidomics study. J. Biol. Chem. 280 (2005) 26796-26804
    • (2005) J. Biol. Chem. , vol.280 , pp. 26796-26804
    • Pike, L.J.1    Han, X.2    Gross, R.W.3
  • 29
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • Douglass A.D., and Vale R.D. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 121 (2005) 937-950
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 30
    • 18044377435 scopus 로고    scopus 로고
    • Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein
    • Hooper N.M. Roles of proteolysis and lipid rafts in the processing of the amyloid precursor protein and prion protein. Biochem. Soc. Trans. 33 (2005) 335-338
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 335-338
    • Hooper, N.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.