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Volumn 42, Issue 8, 2011, Pages 1117-1124

Expression of serine 194-phosphorylated Fas-associated death domain protein correlates with proliferation in B-cell non-Hodgkin lymphomas

Author keywords

B cell; FADD; Lymphomas; Phosphorylation, Proliferation

Indexed keywords

FAS ASSOCIATED DEATH DOMAIN PROTEIN; SERINE;

EID: 79960429920     PISSN: 00468177     EISSN: 15328392     Source Type: Journal    
DOI: 10.1016/j.humpath.2010.11.002     Document Type: Article
Times cited : (12)

References (34)
  • 1
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan A.M., O'Rourke K., Tewari M., and Dixit V.M. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis Cell 81 1995 505 512
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 2
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
    • Boldin M.P., Varfolomeev E.E., Pancer Z., Mett I.L., Camonis J.H., and Wallach D. A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain J Biol Chem 270 1995 7795 7798
    • (1995) J Biol Chem , vol.270 , pp. 7795-7798
    • Boldin, M.P.1    Varfolomeev, E.E.2    Pancer, Z.3    Mett, I.L.4    Camonis, J.H.5    Wallach, D.6
  • 3
    • 19244365798 scopus 로고    scopus 로고
    • The domains of apoptosis: A genomics perspective
    • Reed J.C., Doctor K.S., and Godzik A. The domains of apoptosis: a genomics perspective Sci STKE 2004 2004 re9
    • (2004) Sci STKE , vol.2004 , pp. 9
    • Reed, J.C.1    Doctor, K.S.2    Godzik, A.3
  • 4
    • 0842281645 scopus 로고    scopus 로고
    • Cell Death: Critical Control Points
    • DOI 10.1016/S0092-8674(04)00046-7
    • Danial N.N., and Korsmeyer S.J. Cell death: critical control points Cell 116 2004 205 219 (Pubitemid 38167313)
    • (2004) Cell , vol.116 , Issue.2 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 5
    • 27544432516 scopus 로고    scopus 로고
    • Nonapoptotic functions of FADD-binding death receptors and their signaling molecules
    • DOI 10.1016/j.ceb.2005.09.010, PII S0955067405001390
    • Park S.M., Schickel R., and Peter M.E. Nonapoptotic functions of FADD-binding death receptors and their signaling molecules Curr Opin Cell Biol 17 2005 610 616 (Pubitemid 41540410)
    • (2005) Current Opinion in Cell Biology , vol.17 , Issue.6 , pp. 610-616
    • Park, S.-M.1    Schickel, R.2    Peter, M.E.3
  • 6
    • 33751213356 scopus 로고    scopus 로고
    • Emerging roles for the death adaptor FADD in death receptor avidity and cell cycle regulation
    • Werner M.H., Wu C., and Walsh C.M. Emerging roles for the death receptor FADD in death receptor avidity and cell cycle regulation Cell Cycle 5 2006 2332 2338 (Pubitemid 44785841)
    • (2006) Cell Cycle , vol.5 , Issue.20 , pp. 2332-2338
    • Werner, M.H.1    Wu, C.2    Walsh, C.M.3
  • 7
    • 0034142374 scopus 로고    scopus 로고
    • Phosphorylation of FADD/MORT1 at serine 194 and association with a 70- kDa cell cycle-regulated protein kinase
    • Scaffidi C., Volkland J., Blomberg I., Hoffmann I., Krammer P.H., and Peter M.E. Phosphorylation of FADD/MORT1 at serine 194 and association with a 70-kDa cell cycle-regulated protein kinase J Immunol 164 2000 1236 1242 (Pubitemid 30067235)
    • (2000) Journal of Immunology , vol.164 , Issue.3 , pp. 1236-1242
    • Scaffidi, C.1    Volkland, J.2    Blomberg, I.3    Hoffmann, I.4    Krammer, P.H.5    Peter, M.E.6
  • 8
    • 0037397756 scopus 로고    scopus 로고
    • A function of Fas-associated death domain protein in cell cycle progression localized to a single amino acid at its C-terminal region
    • DOI 10.1016/S1074-7613(03)00083-9
    • Hua Z.C., Sohn S.J., Kang C., Cado D., and Winoto A. A function of Fas-associated death domain protein in cell cycle progression localized to a single amino acid at its C-terminal region Immunity 18 2003 513 521 (Pubitemid 36513633)
    • (2003) Immunity , vol.18 , Issue.4 , pp. 513-521
    • Hua, Z.C.1    Sohn, S.J.2    Kang, C.3    Cado, D.4    Winoto, A.5
  • 9
    • 0142211350 scopus 로고    scopus 로고
    • Cell Cycle Effects by C-FADD Depend on its C-terminal Phosphorylation Site
    • DOI 10.1074/jbc.C300385200
    • Alappat E.C., Volkland J., and Peter M.E. Cell cycle effects by C-FADD depend on its C-terminal phosphorylation site J Biol Chem 278 2003 41585 41588 (Pubitemid 37310412)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.43 , pp. 41585-41588
    • Alappat, E.C.1    Volkland, J.2    Peter, M.E.3
  • 10
    • 9444233897 scopus 로고    scopus 로고
    • FADD and its phosphorylation
    • DOI 10.1080/15216540400008929
    • Zhang J., Zhang D., and Hua Z. FADD and its phosphorylation IUBMB Life 56 2004 395 401 (Pubitemid 39564303)
    • (2004) IUBMB Life , vol.56 , Issue.7 , pp. 395-401
    • Zhang, J.1    Zhang, D.2    Hua, Z.3
  • 12
    • 0034675849 scopus 로고    scopus 로고
    • FIST/HIPK3: A Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits fas-mediated Jun NH(2)-terminal kinase activation
    • Rochat-Steiner V., Becker K., Micheau O., Schneider P., Burns K., and Tschopp J. FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits fas-mediated Jun NH(2)-terminal kinase activation J Exp Med 192 2000 1165 1174
    • (2000) J Exp Med , vol.192 , pp. 1165-1174
    • Rochat-Steiner, V.1    Becker, K.2    Micheau, O.3    Schneider, P.4    Burns, K.5    Tschopp, J.6
  • 15
    • 33344457562 scopus 로고    scopus 로고
    • FADD phosphorylation is critical for cell cycle regulation in breast cancer cells
    • DOI 10.1038/sj.bjc.6602955
    • Matsuyoshi S., Shimada K., Nakamura M., Ishida E., and Konishi N. FADD phosphorylation is critical for cell cycle regulation in breast cancer cells Br J Cancer 94 2006 532 539 (Pubitemid 43289757)
    • (2006) British Journal of Cancer , vol.94 , Issue.4 , pp. 532-539
    • Matsuyoshi, S.1    Shimada, K.2    Nakamura, M.3    Ishida, E.4    Konishi, N.5
  • 16
    • 22644437462 scopus 로고    scopus 로고
    • Phosphorylation status of Fas-associated death domain-containing protein (FADD) is associated with prostate cancer progression
    • DOI 10.1002/path.1791
    • Shimada K., Matsuyoshi S., Nakamura M., Ishida E., and Konishi N. Phosphorylation status of Fas-associated death domain-containing protein (FADD) is associated with prostate cancer progression J Pathol 206 2005 423 432 (Pubitemid 41025345)
    • (2005) Journal of Pathology , vol.206 , Issue.4 , pp. 423-432
    • Shimada, K.1    Matsuyoshi, S.2    Nakamura, M.3    Ishida, E.4    Konishi, N.5
  • 22
    • 0032546387 scopus 로고    scopus 로고
    • Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1
    • Zhang J., Cado D., Chen A., Kabra N.H., and Winoto A. Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1 Nature 392 1998 296 300
    • (1998) Nature , vol.392 , pp. 296-300
    • Zhang, J.1    Cado, D.2    Chen, A.3    Kabra, N.H.4    Winoto, A.5
  • 23
    • 0032472916 scopus 로고    scopus 로고
    • A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes
    • DOI 10.1093/emboj/17.3.706
    • Newton K., Harris A.W., Bath M.L., Smith K.G., and Strasser A. A dominant interfering mutant of FADD/MORT1 enhances deletion of autoreactive thymocytes and inhibits proliferation of mature T lymphocytes EMBO J 17 1998 706 718 (Pubitemid 28062050)
    • (1998) EMBO Journal , vol.17 , Issue.3 , pp. 706-718
    • Newton, K.1    Harris, A.W.2    Bath, M.L.3    Smith, K.G.C.4    Strasser, A.5
  • 24
    • 65649142191 scopus 로고    scopus 로고
    • The death domain of FADD is essential for embryogenesis, lymphocyte development, and proliferation
    • Imtiyaz H.Z., Zhou X., Zhang H., Chen D., Hu T., and Zhang J. The death domain of FADD is essential for embryogenesis, lymphocyte development, and proliferation J Biol Chem 284 2009 9917 9926
    • (2009) J Biol Chem , vol.284 , pp. 9917-9926
    • Imtiyaz, H.Z.1    Zhou, X.2    Zhang, H.3    Chen, D.4    Hu, T.5    Zhang, J.6
  • 26
    • 0040189996 scopus 로고    scopus 로고
    • A dominant negative Fas-associated death domain protein mutant inhibits proliferation and leads to impaired calcium mobilization in both T-cells and fibroblasts
    • DOI 10.1074/jbc.275.14.10453
    • Hueber A.O., Zornig M., Bernard A.M., Chautan M., and Evan G. A dominant negative Fas-associated death domain protein mutant inhibits proliferation and leads to impaired calcium mobilization in both T-cells and fibroblasts J Biol Chem 275 2000 10453 10462 (Pubitemid 30202106)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 10453-10462
    • Hueber, A.-O.1    Zornig, M.2    Bernard, A.-M.3    Chautan, M.4    Evan, G.5
  • 27
    • 27744526076 scopus 로고    scopus 로고
    • Nuclear localized phosphorylated FADD induces cell proliferation and is associated with aggressive lung cancer
    • Bhojani M.S., Chen G., Ross B.D., Beer D.G., and Rehemtulla A. Nuclear localized phosphorylated FADD induces cell proliferation and is associated with aggressive lung cancer Cell Cycle 4 2005 1478 1481
    • (2005) Cell Cycle , vol.4 , pp. 1478-1481
    • Bhojani, M.S.1    Chen, G.2    Ross, B.D.3    Beer, D.G.4    Rehemtulla, A.5
  • 28
    • 3242755146 scopus 로고    scopus 로고
    • Phosphorylation of FADD is critical for sensitivity to anticancer drug-induced apoptosis
    • DOI 10.1093/carcin/bgh130
    • Shimada K., Matsuyoshi S., Nakamura M., Ishida E., Kishi M., and Konishi N. Phosphorylation of FADD is critical for sensitivity to anticancer drug-induced apoptosis Carcinogenesis 25 2004 1089 1097 (Pubitemid 38968037)
    • (2004) Carcinogenesis , vol.25 , Issue.7 , pp. 1089-1097
    • Shimada, K.1    Matsuyoshi, S.2    Nakamura, M.3    Ishida, E.4    Kishi, M.5    Konishi, N.6
  • 30
    • 85078505221 scopus 로고    scopus 로고
    • The FADD is going nuclear
    • Sheikh M.S., and Huang Y. The FADD is going nuclear Cell Cycle 2 2003 346 347
    • (2003) Cell Cycle , vol.2 , pp. 346-347
    • Sheikh, M.S.1    Huang, Y.2
  • 31
    • 0038494553 scopus 로고    scopus 로고
    • Molecular evidence for the nuclear localization of FADD
    • DOI 10.1038/sj.cdd.4401237
    • Gomez-Angelats M., and Cidlowski J.A. Molecular evidence for the nuclear localization of FADD Cell Death Differ 10 2003 791 797 (Pubitemid 36850240)
    • (2003) Cell Death and Differentiation , vol.10 , Issue.7 , pp. 791-797
    • Gomez-Angelats, M.1    Cidlowski, J.A.2
  • 33
    • 2342443733 scopus 로고    scopus 로고
    • JNK Regulates HIPK3 Expression and Promotes Resistance to Fas-mediated Apoptosis in DU 145 Prostate Carcinoma Cells
    • DOI 10.1074/jbc.M307629200
    • Curtin J.F., and Cotter T.G. JNK regulates HIPK3 expression and promotes resistance to Fas-mediated apoptosis in DU 145 prostate carcinoma cells J Biol Chem 279 2004 17090 17100 (Pubitemid 38560465)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17090-17100
    • Curtin, J.F.1    Cotter, T.G.2
  • 34


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.