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Volumn 123, Issue 15, 2010, Pages 2596-2604

p38γ regulates interaction of nuclear PSF and RNA with the tumour-suppressor hDlg in response to osmotic shock

Author keywords

hDlg; Inactive p38 ; Knock in mice; Osmotic shock; p38 ; PSF

Indexed keywords

DISC LARGE PROTEIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE 12; NUCLEAR PROTEIN; POLYPYRIMIDINE TRACT BINDING PROTEIN; PROTEIN ASSOCIATED SPLICING FACTOR; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG; DLG1 PROTEIN, HUMAN; MEMBRANE PROTEIN; PTB ASSOCIATED SPLICING FACTOR; PTB-ASSOCIATED SPLICING FACTOR; RNA; RNA BINDING PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 77955371720     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.066514     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 0035012401 scopus 로고    scopus 로고
    • Stress-induced MAP kinase Hog1 is part of transcription activation complexes
    • DOI 10.1016/S1097-2765(01)00221-0
    • Alepuz, P. M., Jovanovic, A., Reiser, V. and Ammerer, G. (2001). Stress-induced map kinase Hog1 is part of transcription activation complexes. Mol. Cell 7, 767-777. (Pubitemid 32436437)
    • (2001) Molecular Cell , vol.7 , Issue.4 , pp. 767-777
    • Alepuz, P.M.1    Jovanovic, A.2    Reiser, V.3    Ammerer, G.4
  • 2
    • 0034595219 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression
    • Balda, M. S. and Matter, K. (2000). The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression. EMBO J. 19, 2024-2033.
    • (2000) EMBO J , vol.19 , pp. 2024-2033
    • Balda, M.S.1    Matter, K.2
  • 3
    • 0037134020 scopus 로고    scopus 로고
    • A system for stable expression of short interfering RNAs in mammalian cells
    • DOI 10.1126/science.1068999
    • Brummelkamp, T. R., Bernards, R. and Agami, R. (2002). A system for stable expression of short interfering RNAs in mammalian cells. Science 296, 550-553. (Pubitemid 34408678)
    • (2002) Science , vol.296 , Issue.5567 , pp. 550-553
    • Brummelkamp, T.R.1    Bernards, R.2    Agami, R.3
  • 4
    • 35648982347 scopus 로고    scopus 로고
    • Cellular response to hyperosmotic stresses
    • Burg, M. B., Ferraris, J. D. and Dmitrieva, N. I. (2007). Cellular response to hyperosmotic stresses. Physiol. Rev. 87, 1441-1474.
    • (2007) Physiol. Rev. , vol.87 , pp. 1441-1474
    • Burg, M.B.1    Ferraris, J.D.2    Dmitrieva, N.I.3
  • 5
    • 38049153326 scopus 로고    scopus 로고
    • The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha
    • Buxade, M., Morrice, N., Krebs, D. L. and Proud, C. G. (2008). The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha. J. Biol. Chem. 283, 57-65.
    • (2008) J. Biol. Chem. , vol.283 , pp. 57-65
    • Buxade, M.1    Morrice, N.2    Krebs, D.L.3    Proud, C.G.4
  • 7
    • 34547154349 scopus 로고    scopus 로고
    • P38 MAP-Kinases pathway regulation, function and role in human diseases
    • DOI 10.1016/j.bbamcr.2007.03.010, PII S0167488907000705
    • Cuenda, A. and Rousseau, S. (2007). p38 MAP-kinases pathway regulation, function and role in human diseases. Biochim. Biophys. Acta 1773, 1358-1375. (Pubitemid 47125981)
    • (2007) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1773 , Issue.8 , pp. 1358-1375
    • Cuenda, A.1    Rousseau, S.2
  • 8
    • 0031024646 scopus 로고    scopus 로고
    • Activation of stress-activated protein kinase-3 (SAPK3) by cytokines and cellular stresses is mediated via SAPKK3 (MKK6); Comparison of the specificities of SAPK3 and SAPK2 (RK/p38)
    • DOI 10.1093/emboj/16.2.295
    • Cuenda, A., Cohen, P., Buee-Scherrer, V. and Goedert, M. (1997). Activation of stress-activated protein kinase-3 (SAPK3) by cytokines and cellular stresses is mediated via SAPKK3 (MKK6); comparison of the specificities of SAPK3 and SAPK2 (RK/p38). EMBO J. 16, 295-305. (Pubitemid 27049387)
    • (1997) EMBO Journal , vol.16 , Issue.2 , pp. 295-305
    • Cuenda, A.1    Cohen, P.2    Buee-Scherrer, V.3    Goedert, M.4
  • 11
    • 22244455455 scopus 로고    scopus 로고
    • Membrane-associated guanylate kinases regulate adhesion and plasticity at cell junctions
    • DOI 10.1146/annurev.biochem.74.082803.133339
    • Funke, L., Dakoji, S. and Bredt, D. S. (2005). Membrane-associated guanylate kinases regulate adhesion and plasticity at cell junctions. Annu. Rev. Biochem. 74, 219-245. (Pubitemid 40995507)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 219-245
    • Funke, L.1    Dakoji, S.2    Bredt, D.S.3
  • 12
    • 37549064721 scopus 로고    scopus 로고
    • The nuclear RhoA exchange factor Net1 interacts with proteins of the Dlg family, affects their localization, and influences their tumor suppressor activity
    • Garcia-Mata, R., Dubash, A. D., Sharek, L., Carr, H. S., Frost, J. A. and Burridge, K. (2007). The nuclear RhoA exchange factor Net1 interacts with proteins of the Dlg family, affects their localization, and influences their tumor suppressor activity. Mol. Cell. Biol. 27, 8683-8697.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8683-8697
    • Garcia-Mata, R.1    Dubash, A.D.2    Sharek, L.3    Carr, H.S.4    Frost, J.A.5    Burridge, K.6
  • 13
    • 0030927106 scopus 로고    scopus 로고
    • Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison of its substrate specificity with that of other SAP kinases
    • Goedert, M., Cuenda, A., Craxton, M., Jakes, R. and Cohen, P. (1997). Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison of its substrate specificity with that of other SAP kinases. EMBO J. 16, 3563-3571.
    • (1997) EMBO J , vol.16 , pp. 3563-3571
    • Goedert, M.1    Cuenda, A.2    Craxton, M.3    Jakes, R.4    Cohen, P.5
  • 14
    • 0033617341 scopus 로고    scopus 로고
    • Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin. A mechanism for specific substrate recognition
    • Hasegawa, M., Cuenda, A., Spillantini, M. G., Thomas, G. M., Buee-Scherrer, V., Cohen, P. and Goedert, M. (1999). Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin. A mechanism for specific substrate recognition. J. Biol. Chem. 274, 12626-12631.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12626-12631
    • Hasegawa, M.1    Cuenda, A.2    Spillantini, M.G.3    Thomas, G.M.4    Buee-Scherrer, V.5    Cohen, P.6    Goedert, M.7
  • 16
    • 0034673760 scopus 로고    scopus 로고
    • Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
    • Hsueh, Y. P., Wang, T. F., Yang, F. C. and Sheng, M. (2000). Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2. Nature 404, 298-302.
    • (2000) Nature , vol.404 , pp. 298-302
    • Hsueh, Y.P.1    Wang, T.F.2    Yang, F.C.3    Sheng, M.4
  • 17
    • 0038795589 scopus 로고    scopus 로고
    • Dlg, scribble and Lgl in cell polarity, cell proliferation and cancer
    • DOI 10.1002/bies.10286
    • Humbert, P., Russell, S. and Richardson, H. (2003). Dlg, Scribble and Lgl in cell polarity, cell proliferation and cancer. BioEssays 25, 542-553. (Pubitemid 36702323)
    • (2003) BioEssays , vol.25 , Issue.6 , pp. 542-553
    • Humbert, P.1    Russell, S.2    Richardson, H.3
  • 18
    • 58149172028 scopus 로고    scopus 로고
    • Proteolysis of the tumour suppressor hDlg in response to osmotic stress is mediated by caspases and independent of phosphorylation
    • Inesta-Vaquera, F. A., Centeno, F., del Reino, P., Sabio, G., Peggie, M. and Cuenda, A. (2009). Proteolysis of the tumour suppressor hDlg in response to osmotic stress is mediated by caspases and independent of phosphorylation. FEBS J. 276, 387-400.
    • (2009) FEBS J , vol.276 , pp. 387-400
    • Inesta-Vaquera, F.A.1    Centeno, F.2    Del Reino, P.3    Sabio, G.4    Peggie, M.5    Cuenda, A.6
  • 19
    • 0035881737 scopus 로고    scopus 로고
    • A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta
    • Knebel, A., Morrice, N. and Cohen, P. (2001). A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta. EMBO J. 20, 4360-4369.
    • (2001) EMBO J , vol.20 , pp. 4360-4369
    • Knebel, A.1    Morrice, N.2    Cohen, P.3
  • 20
    • 33750117119 scopus 로고    scopus 로고
    • Maintenance and modulation of T cell polarity
    • Krummel, M. F. and Macara, I. (2006). Maintenance and modulation of T cell polarity. Nat. Immunol. 7, 1143-1149.
    • (2006) Nat. Immunol. , vol.7 , pp. 1143-1149
    • Krummel, M.F.1    Macara, I.2
  • 22
    • 1642342675 scopus 로고    scopus 로고
    • Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells
    • Laprise, P., Viel, A. and Rivard, N. (2004). Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells. J. Biol. Chem. 279, 10157-10166.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10157-10166
    • Laprise, P.1    Viel, A.2    Rivard, N.3
  • 23
    • 33846783268 scopus 로고    scopus 로고
    • Dual role of CaMKII-dependent SAP97 phosphorylation in mediating trafficking and insertion of NMDA receptor subunit NR2A
    • DOI 10.1111/j.1471-4159.2006.04267.x
    • Mauceri, D., Gardoni, F., Marcello, E. and Di Luca, M. (2007). Dual role of CaMKII-dependent SAP97 phosphorylation in mediating trafficking and insertion of NMDA receptor subunit NR2A. J. Neurochem. 100, 1032-1046. (Pubitemid 46213927)
    • (2007) Journal of Neurochemistry , vol.100 , Issue.4 , pp. 1032-1046
    • Mauceri, D.1    Gardoni, F.2    Marcello, E.3    Di Luca, M.4
  • 24
    • 0036289351 scopus 로고    scopus 로고
    • Hog1 kinase converts the Sko1-Cyc8-Tup1 repressor complex into an activator that recruits SAGA and SWI/SNF in response to osmotic stress
    • Proft, M. and Struhl, K. (2002). Hog1 kinase converts the Sko1-Cyc8-Tup1 repressor complex into an activator that recruits SAGA and SWI/SNF in response to osmotic stress. Mol. Cell 9, 1307-1317.
    • (2002) Mol. Cell , vol.9 , pp. 1307-1317
    • Proft, M.1    Struhl, K.2
  • 25
    • 34250801537 scopus 로고    scopus 로고
    • Changes in localization of human discs large (hDlg) during keratinocyte differentiation is associated with expression of alternatively spliced hDlg variants
    • DOI 10.1016/j.yexcr.2007.05.017, PII S0014482707002455
    • Roberts, S., Calautti, E., Vanderweil, S., Nguyen, H. O., Foley, A., Baden, H. P. and Viel, A. (2007). Changes in localization of human discs large (hDlg) during keratinocyte differentiation are [corrected] associated with expression of alternatively spliced hDlg variants. Exp. Cell Res. 313, 2521-2530. (Pubitemid 46977350)
    • (2007) Experimental Cell Research , vol.313 , Issue.12 , pp. 2521-2530
    • Roberts, S.1    Calautti, E.2    Vanderweil, S.3    Nguyen, H.O.4    Foley, A.5    Baden, H.P.6    Viel, A.7
  • 26
    • 0037011121 scopus 로고    scopus 로고
    • Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAPK2 and its interaction with cytokine mRNAs
    • Rousseau, S., Morrice, N., Peggie, M., Campbell, D. G., Gaestel, M. and Cohen, P. (2002). Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAPK2 and its interaction with cytokine mRNAs. EMBO J. 21, 6505-6514.
    • (2002) EMBO J , vol.21 , pp. 6505-6514
    • Rousseau, S.1    Morrice, N.2    Peggie, M.3    Campbell, D.G.4    Gaestel, M.5    Cohen, P.6
  • 27
    • 2442637022 scopus 로고    scopus 로고
    • Stress- And mitogen-induced phosphorylation of the synapse-associated protein SAP90/PSD-95 by activation of SAPK3/p38gamma and ERK1/ERK2
    • Sabio, G., Reuver, S., Feijoo, C., Hasegawa, M., Thomas, G. M., Centeno, F., Kuhlendahl, S., Leal-Ortiz, S., Goedert, M., Garner, C. et al. (2004). Stress- and mitogen-induced phosphorylation of the synapse-associated protein SAP90/PSD-95 by activation of SAPK3/p38gamma and ERK1/ERK2. Biochem. J. 380, 19-30.
    • (2004) Biochem. J. , vol.380 , pp. 19-30
    • Sabio, G.1    Reuver, S.2    Feijoo, C.3    Hasegawa, M.4    Thomas, G.M.5    Centeno, F.6    Kuhlendahl, S.7    Leal-Ortiz, S.8    Goedert, M.9    Garner, C.10
  • 29
    • 0037032415 scopus 로고    scopus 로고
    • PSF and p54(nrb)/NonO-multi-functional nuclear proteins
    • Shav-Tal, Y. and Zipori, D. (2002). PSF and p54(nrb)/NonO-multi- functional nuclear proteins. FEBS Lett. 531, 109-114.
    • (2002) FEBS Lett , vol.531 , pp. 109-114
    • Shav-Tal, Y.1    Zipori, D.2
  • 30
    • 21244490119 scopus 로고    scopus 로고
    • Essential role of p38gamma in K-ras transformation independent of phosphorylation
    • DOI 10.1074/jbc.M500699200
    • Tang, J., Qi, X., Mercola, D., Han, J. and Chen, G. (2005). Essential role of p38gamma in K-Ras transformation independent of phosphorylation. J. Biol. Chem. 280, 23910-23917. (Pubitemid 40884879)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 23910-23917
    • Tang, J.1    Qi, X.2    Mercola, D.3    Han, J.4    Chen, G.5


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