메뉴 건너뛰기




Volumn 110, Issue 5, 2013, Pages

Activation of NF-κB signalling by fusicoccin-induced dimerization

Author keywords

Cell biology; Fluorescence microscopy; Protein engineering; Protein protein interaction; Surface plasmon resonance

Indexed keywords

FUSICOCCIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 8; PROTEIN 14 3 3;

EID: 84873194912     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1212990110     Document Type: Article
Times cited : (35)

References (35)
  • 1
    • 0027756895 scopus 로고
    • Controlling signal transduction with synthetic ligands
    • Spencer DM, Wandless TJ, Schreiber SL, Crabtree GR (1993) Controlling signal transduction with synthetic ligands. Science 262(5136):1019-1024. (Pubitemid 24035037)
    • (1993) Science , vol.262 , Issue.5136 , pp. 1019-1024
    • Spencer, D.M.1    Wandless, T.J.2    Schreiber, S.L.3    Crabtree, G.R.4
  • 2
    • 0029737867 scopus 로고    scopus 로고
    • Dimeric ligands define a role for transcriptional activation domains in reinitiation
    • DOI 10.1038/382822a0
    • Ho SN, Biggar SR, Spencer DM, Schreiber SL, Crabtree GR (1996) Dimeric ligands define a role for transcriptional activation domains in reinitiation. Nature 382(6594):822-826. (Pubitemid 26299568)
    • (1996) Nature , vol.382 , Issue.6594 , pp. 822-826
    • Ho, S.N.1    Biggar, S.R.2    Spencer, D.M.3    Schreiber, S.L.4    Crabtree, G.R.5
  • 4
    • 84863627544 scopus 로고    scopus 로고
    • Protein translocation as a tool: The current rapamycin story
    • Putyrski M, Schultz C (2012) Protein translocation as a tool: The current rapamycin story. FEBS Lett 586(15):2097-2105.
    • (2012) FEBS Lett , vol.586 , Issue.15 , pp. 2097-2105
    • Putyrski, M.1    Schultz, C.2
  • 8
    • 0029807304 scopus 로고    scopus 로고
    • Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization
    • DOI 10.1038/383178a0
    • Farrar MA, Alberol-Ila J, Perlmutter RM (1996) Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization. Nature 383(6596):178-181. (Pubitemid 26303982)
    • (1996) Nature , vol.383 , Issue.6596 , pp. 178-181
    • Farrar, M.A.1    Alberola-Ila, J.2    Perlmutter, R.M.3
  • 9
    • 79952773870 scopus 로고    scopus 로고
    • Engineering the ABA plant stress pathway for regulation of induced proximity
    • Liang F-S, Ho WQ, Crabtree GR (2011) Engineering the ABA plant stress pathway for regulation of induced proximity. Sci Signal 4(164):rs2.
    • (2011) Sci Signal , vol.4 , Issue.164
    • Liang, F.-S.1    Ho, W.Q.2    Crabtree, G.R.3
  • 10
    • 84862815933 scopus 로고    scopus 로고
    • Rapid and orthogonal logic gating with a gibberellininduced dimerization system
    • Miyamoto T, et al. (2012) Rapid and orthogonal logic gating with a gibberellininduced dimerization system. Nat Chem Biol 8(5):465-470.
    • (2012) Nat Chem Biol , vol.8 , Issue.5 , pp. 465-470
    • Miyamoto, T.1
  • 11
    • 0000765578 scopus 로고
    • Fusicoccin: A new wilting toxin produced by Fusicoccum amygdali del
    • Ballio A, et al. (1964) Fusicoccin: A new wilting toxin produced by Fusicoccum amygdali del. Nature 203:297-297.
    • (1964) Nature , vol.203 , pp. 297-297
    • Ballio, A.1
  • 12
    • 0037416221 scopus 로고    scopus 로고
    • Structural view of a fungal toxin acting on a 14-3-3 regulatory complex
    • DOI 10.1093/emboj/cdg104
    • Würtele M, Jelich-Ottmann C, Wittinghofer A, Oecking C (2003) Structural view of a fungal toxin acting on a 14-3-3 regulatory complex. EMBO J 22(5):987-994. (Pubitemid 36313583)
    • (2003) EMBO Journal , vol.22 , Issue.5 , pp. 987-994
    • Wurtele, M.1    Jelich-Ottmann, C.2    Wittinghofer, A.3    Oecking, C.4
  • 14
    • 33744544172 scopus 로고    scopus 로고
    • 14-3-3 proteins in cell cycle regulation
    • DOI 10.1016/j.semcancer.2006.03.002, PII S1044579X06000265
    • Hermeking H, Benzinger A (2006) 14-3-3 proteins in cell cycle regulation. Semin Cancer Biol 16(3):183-192. (Pubitemid 43810261)
    • (2006) Seminars in Cancer Biology , vol.16 , Issue.3 , pp. 183-192
    • Hermeking, H.1    Benzinger, A.2
  • 15
    • 33644877400 scopus 로고    scopus 로고
    • 14-3-3 proteins: A number of functions for a numbered protein
    • Bridges D, Moorhead GBG (2005) 14-3-3 proteins: A number of functions for a numbered protein. Sci STKE 2005(296):re10.
    • (2005) Sci STKE , vol.2005 , Issue.296
    • Bridges, D.1    Moorhead, G.B.G.2
  • 16
    • 58149488988 scopus 로고    scopus 로고
    • The 14-3-3 proteins: Integrators of diverse signaling cues that impact cell fate and cancer development
    • Morrison DK (2009) The 14-3-3 proteins: Integrators of diverse signaling cues that impact cell fate and cancer development. Trends Cell Biol 19(1):16-23.
    • (2009) Trends Cell Biol , vol.19 , Issue.1 , pp. 16-23
    • Morrison, D.K.1
  • 19
    • 77950872530 scopus 로고    scopus 로고
    • Bioinformatic and experimental survey of 14-3-3-binding sites
    • Johnson C, et al. (2010) Bioinformatic and experimental survey of 14-3-3-binding sites. Biochem J 427(1):69-78.
    • (2010) Biochem J , vol.427 , Issue.1 , pp. 69-78
    • Johnson, C.1
  • 20
    • 0033180582 scopus 로고    scopus 로고
    • Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding
    • DOI 10.1016/S1097-2765(00)80363-9
    • Rittinger K, et al. (1999) Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding. Mol Cell 4(2):153-166. (Pubitemid 29456884)
    • (1999) Molecular Cell , vol.4 , Issue.2 , pp. 153-166
    • Rittinger, K.1    Budman, J.2    Xu, J.3    Volinia, S.4    Cantley, L.C.5    Smerdon, S.J.6    Gamblin, S.J.7    Yaffe, M.B.8
  • 21
    • 77956687588 scopus 로고    scopus 로고
    • Impaired binding of 14-3-3 to C-RAF in Noonan syndrome suggests new approaches in diseases with increased Ras signaling
    • Molzan M, et al. (2010) Impaired binding of 14-3-3 to C-RAF in Noonan syndrome suggests new approaches in diseases with increased Ras signaling. Mol Cell Biol 30(19):4698-4711.
    • (2010) Mol Cell Biol , vol.30 , Issue.19 , pp. 4698-4711
    • Molzan, M.1
  • 22
    • 0029101592 scopus 로고
    • 14-3-3 proteins associate with cdc25 phosphatases
    • Conklin DS, Galaktionov K, Beach D (1995) 14-3-3 proteins associate with cdc25 phosphatases. Proc Natl Acad Sci USA 92(17):7892-7896.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.17 , pp. 7892-7896
    • Conklin, D.S.1    Galaktionov, K.2    Beach, D.3
  • 23
    • 0035873391 scopus 로고    scopus 로고
    • TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm
    • DOI 10.1101/gad.888601
    • Vassilev A, Kaneko KJ, Shu H, Zhao Y, De Pamphilis ML (2001) TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm. Genes Dev 15(10):1229-1241. (Pubitemid 32472752)
    • (2001) Genes and Development , vol.15 , Issue.10 , pp. 1229-1241
    • Vassilev, A.1    Kaneko, K.J.2    Shu, H.3    Zhao, Y.4    DePamphilis, M.L.5
  • 25
    • 0037112329 scopus 로고    scopus 로고
    • Forward transport: 14-3-3 Binding overcomes retention in endoplasmic reticulum by dibasic signals
    • DOI 10.1016/S0092-8674(02)01040-1
    • O'Kelly I, Butler MH, Zilberberg N, Goldstein SAN (2002) Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals. Cell 111(4):577-588. (Pubitemid 35356562)
    • (2002) Cell , vol.111 , Issue.4 , pp. 577-588
    • O'Kelly, I.1    Butler, M.H.2    Zilberberg, N.3    Goldstein, S.A.N.4
  • 26
    • 9644266572 scopus 로고    scopus 로고
    • Cdc25A localisation and shuttling: Characterisation of sequences mediating nuclear export and import
    • DOI 10.1016/j.yexcr.2004.09.012, PII S0014482704005373
    • Källström H, Lindqvist A, Pospisil V, Lundgren A, Rosenthal CK (2005) Cdc25A localisation and shuttling: Characterisation of sequences mediating nuclear export and import. Exp Cell Res 303(1):89-100. (Pubitemid 39575147)
    • (2005) Experimental Cell Research , vol.303 , Issue.1 , pp. 89-100
    • Kallstrom, H.1    Lindqvist, A.2    Pospisil, V.3    Lundgren, A.4    Rosenthal, C.K.5
  • 27
    • 0021285532 scopus 로고
    • A short sequence in the p60(src) N terminus is required for p60(src) myristylation and membrane association and for cell transformation
    • Cross FR, Garber EA, Pellman D, Hanafusa H (1984) A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation. Mol Cell Biol 4(9):1834-1842. (Pubitemid 14008294)
    • (1984) Molecular and Cellular Biology , vol.4 , Issue.9 , pp. 1834-1842
    • Cross, F.R.1    Garber, E.A.2    Pellman, D.3    Hanafusa, H.4
  • 29
    • 0027332498 scopus 로고
    • The I κ B proteins: Multifunctional regulators of Rel/NF-κ B transcription factors
    • Beg AA, Baldwin AS, Jr. (1993) The I κ B proteins: Multifunctional regulators of Rel/NF-κ B transcription factors. Genes Dev 7(11):2064-2070.
    • (1993) Genes Dev , vol.7 , Issue.11 , pp. 2064-2070
    • Beg, A.A.1    Baldwin Jr., A.S.2
  • 30
    • 11844251170 scopus 로고    scopus 로고
    • The NF-κB/IκB signaling system: A molecular target in breast cancer therapy
    • DOI 10.1016/j.jss.2004.06.006, PII S0022480404002562
    • Wu JT, Kral JG (2005) The NF-kappaB/IkappaB signaling system: A molecular target in breast cancer therapy. J Surg Res 123(1):158-169. (Pubitemid 40094658)
    • (2005) Journal of Surgical Research , vol.123 , Issue.1 , pp. 158-169
    • Wu, J.T.1    Kral, J.G.2
  • 31
    • 53549131018 scopus 로고    scopus 로고
    • Conditional glycosylation in eukaryotic cells using a biocompatible chemical inducer of dimerization
    • Czlapinski JL, et al. (2008) Conditional glycosylation in eukaryotic cells using a biocompatible chemical inducer of dimerization. J Am Chem Soc 130(40):13186-13187.
    • (2008) J Am Chem Soc , vol.130 , Issue.40 , pp. 13186-13187
    • Czlapinski, J.L.1
  • 32
    • 0036794093 scopus 로고    scopus 로고
    • 14-3-3 Regulates actin dynamics by stabilizing phosphorylated cofilin
    • DOI 10.1016/S0960-9822(02)01184-3, PII S0960982202011843
    • Gohla A, Bokoch GM (2002) 14-3-3 regulates actin dynamics by stabilizing phosphorylated cofilin. Curr Biol 12(19):1704-1710. (Pubitemid 35161927)
    • (2002) Current Biology , vol.12 , Issue.19 , pp. 1704-1710
    • Gohla, A.1    Bokoch, G.M.2
  • 33
    • 3242749629 scopus 로고    scopus 로고
    • The 14-3-3 protein ε isoform expressed in reactive astrocytes in demyelinating lesions of multiple sclerosis binds to vimentin and glial fibrillary acidic protein in cultured human astrocytes
    • Satoh J-I, Yamamura T, Arima K (2004) The 14-3-3 protein epsilon isoform expressed in reactive astrocytes in demyelinating lesions of multiple sclerosis binds to vimentin and glial fibrillary acidic protein in cultured human astrocytes. Am J Pathol 165(2):577-592. (Pubitemid 38971387)
    • (2004) American Journal of Pathology , vol.165 , Issue.2 , pp. 577-592
    • Satoh, J.-I.1    Yamamura, T.2    Arima, K.3
  • 34
    • 16344373193 scopus 로고    scopus 로고
    • Isoform-specific subcellular localization among 14-3-3 proteins in Arabidopsis seems to be driven by client interactions
    • DOI 10.1091/mbc.E04-09-0839
    • Paul A-L, Sehnke PC, Ferl RJ (2005) Isoform-specific subcellular localization among 14-3-3 proteins in Arabidopsis seems to be driven by client interactions. Mol Biol Cell 16(4):1735-1743. (Pubitemid 40471944)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.4 , pp. 1735-1743
    • Paul, A.-L.1    Sehnke, P.C.2    Ferl, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.