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Volumn 8, Issue 22, 2009, Pages 3648-3651

Hacking RNA: Hakai promotes tumorigenesis by enhancing the RNA-binding function of PSF

Author keywords

E cadherin; Oncogene; Proliferation; PSF; PTB associated splicing factor; RNA binding protein; Tumor progression

Indexed keywords

HAKAI PROTEIN; MESSENGER RNA; POLYPYRIMIDINE TRACT BINDING PROTEIN; POLYPYRIMIDINE TRACT BINDING PROTEIN ASSOCIATED SPLICING FACTOR; RING FINGER PROTEIN; RING FINGER PROTEIN 43; RNA; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; UVOMORULIN;

EID: 70449781494     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.8.22.9909     Document Type: Review
Times cited : (33)

References (31)
  • 2
    • 11144296871 scopus 로고    scopus 로고
    • Lysosomal targeting of E-cadherin: A unique mechanism for the down-regulation of cell-cell adhesion during epithelial to mesenchymal transitions
    • DOI 10.1128/MCB.25.1.389-402.2005
    • Palacios F, Tushir JS, Fujita Y, D'Souza-Schorey C. Lysosomal targeting of E-cadherin: a unique mechanism for the downregulation of cell-cell adhesion during epithelial to mesenchymal transitions. Mol Cell Biol 2005; 25:389-402. (Pubitemid 40039828)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.1 , pp. 389-402
    • Palacios, F.1    Tushir, J.S.2    Fujita, Y.3    D'Souza-Schorey, C.4
  • 3
    • 41949117520 scopus 로고    scopus 로고
    • CDC42 regulates E-cadherin ubiquitination and degradation through an EGF receptor to SRC-mediated pathway
    • Shen Y, Hirsch DS, Sasiela CA, Wu WJ. CDC42 regulates E-cadherin ubiquitination and degradation through an EGF receptor to SRC-mediated pathway. J Biol Chem 2007; 283:5127-5137
    • (2007) J Biol Chem , vol.283 , pp. 5127-5137
    • Shen, Y.1    Hirsch, D.S.2    Sasiela, C.A.3    Wu, W.J.4
  • 4
    • 54149096777 scopus 로고    scopus 로고
    • Successive post-translational modifications of E-cadherin are required for InlA-mediated internalisation of Listeria monocytogenes
    • Bonazzi M, Veiga E, Cerda JP, Cossart P. Successive post-translational modifications of E-cadherin are required for InlA-mediated internalisation of Listeria monocytogenes. Cell Microbiol 2008; 10:2208-2222
    • (2008) Cell Microbiol , vol.10 , pp. 2208-2222
    • Bonazzi, M.1    Veiga, E.2    Cerda, J.P.3    Cossart, P.4
  • 5
    • 0027685701 scopus 로고
    • Cadherins in cancer: Implications for invasion and metastasis
    • Takeichi M. Cadherins in cancer: implications for invasion and metastasis. Curr Opin Cell Biol 1993; 5:806-811 (Pubitemid 223002751)
    • (1993) Current Opinion in Cell Biology , vol.5 , Issue.5 , pp. 806-811
    • Takeichi, M.1
  • 6
    • 0028245813 scopus 로고
    • Cadherin expression in carcinomas: Role in the formation of cell junctions and the prevention of invasiveness
    • DOI 10.1016/0304-419X(94)90003-5
    • Birchmeier W, Behrens J. Cadherin expression in carcinomas: role in the formation of cell junctions and the prevention of invasiveness. Biochim Biophys Acta 1994; 1198:11-26. (Pubitemid 24159061)
    • (1994) Biochimica et Biophysica Acta - Reviews on Cancer , vol.1198 , Issue.1 , pp. 11-26
    • Birchmeier, W.1    Behrens, J.2
  • 7
    • 0037459077 scopus 로고    scopus 로고
    • Sticky business: Orchestrating cellular signals at adherens junctions
    • DOI 10.1016/S0092-8674(03)00108-9
    • Perez-Moreno M, Jamora C, Fuchs E. Sticky business: orchestrating cellular signals at adherens junctions. Cell 2003; 112:535-548 (Pubitemid 36263085)
    • (2003) Cell , vol.112 , Issue.4 , pp. 535-548
    • Perez-Moreno, M.1    Jamora, C.2    Fuchs, E.3
  • 9
    • 0036222482 scopus 로고    scopus 로고
    • E-cadherin and Hakai: Signalling, remodeling or destruction?
    • Pece S, Gutkind JS. E-cadherin and Hakai: signalling, remodeling or destruction? Nat Cell Biol 2002; 4:72-74
    • (2002) Nat Cell Biol , vol.4 , pp. 72-74
    • Pece, S.1    Gutkind, J.S.2
  • 12
    • 0031039425 scopus 로고    scopus 로고
    • The intracisternal A-particle proximal enhancer-binding protein activates transcription and is identical to the RNA- And DNA-binding protein p54(nrb)/NonO
    • Basu A, Dong B, Krainer AR, Howe CC. The intracisternal A-particle proximal enhancer-binding protein activates transcription and is identical to the RNA- and DNA-binding protein p54nrb/NonO. Mol Cell Biol 1997; 17:677-686 (Pubitemid 27044367)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.2 , pp. 677-686
    • Basu, A.1    Dong, B.2    Krainer, A.R.3    Howe, C.C.4
  • 13
    • 0035106562 scopus 로고    scopus 로고
    • PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors
    • DOI 10.1128/MCB.21.7.2298-2311.2001
    • Mathur M, Tucker PW, Samuels HH. PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors. Mol Cell Biol 2001; 21:2298-2311 (Pubitemid 32222084)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.7 , pp. 2298-2311
    • Mathur, M.1    Tucker, P.W.2    Samuels, H.H.3
  • 15
    • 34347332370 scopus 로고    scopus 로고
    • Transcriptional activity of androgen receptor is modulated by two RNA splicing factors, PSF and p54nrb
    • Dong X, Sweet J, Challis JR, Brown T, Lye SJ. Transcriptional activity of androgen receptor is modulated by two RNA splicing factors, PSF and p54nrb. Mol Cell Biol 2007; 27:4863-4875
    • (2007) Mol Cell Biol , vol.27 , pp. 4863-4875
    • Dong, X.1    Sweet, J.2    Challis, J.R.3    Brown, T.4    Lye, S.J.5
  • 16
    • 34447550769 scopus 로고    scopus 로고
    • The multifunctional protein p54nrb/PSF recruits the exonuclease XRN2 to facilitate pre-mRNA 3′ processing and transcription termination
    • DOI 10.1101/gad.1565207
    • Kaneko S, Rozenblatt-Rosen O, Meyerson M, Manley JL. The multifunctional protein p54nrb/PSF recruits the exonuclease XRN2 to facilitate pre-mRNA 3′ processing and transcription termination. Genes Dev 2007; 21:1779-1789 (Pubitemid 47076477)
    • (2007) Genes and Development , vol.21 , Issue.14 , pp. 1779-1789
    • Kaneko, S.1    Rozenblatt-Rosen, O.2    Meyerson, M.3    Manley, J.L.4
  • 17
    • 34748892292 scopus 로고    scopus 로고
    • Combinatorial control of signal-induced exon repression by hnRNP L and PSF
    • DOI 10.1128/MCB.00419-07
    • Melton AA, Jackson J, Wang J, Lynch KW. Combinatorial control of signal-induced exon repression by hnRNP L and PSF. Mol Cell Biol 2007; 27:6972-6984 (Pubitemid 47483644)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.19 , pp. 6972-6984
    • Melton, A.A.1    Jackson, J.2    Wang, J.3    Lynch, K.W.4
  • 18
    • 37549036329 scopus 로고    scopus 로고
    • Identification of internal ribosome entry segment (IRES)-trans-acting factors for the Myc family of IRESs
    • Cobbold LC, Spriggs KA, Haines SJ, Dobbyn HC, Hayes C, de Moor CH, et al. Identification of internal ribosome entry segment (IRES)-trans-acting factors for the Myc family of IRESs. Mol Cell Biol 2008; 28:40-49
    • (2008) Mol Cell Biol , vol.28 , pp. 40-49
    • Cobbold, L.C.1    Spriggs, K.A.2    Haines, S.J.3    Dobbyn, H.C.4    Hayes, C.5    De Moor, C.H.6
  • 19
    • 0037032415 scopus 로고    scopus 로고
    • nrb/NonO - Multi-functional nuclear proteins
    • DOI 10.1016/S0014-5793(02)03447-6, PII S0014579302034476
    • Shav-Tal Y, Zipori D. PSF and p54(nrb)/NonO- multi-functional nuclear proteins. FEBS Lett 2002; 531:109-114 (Pubitemid 35341179)
    • (2002) FEBS Letters , vol.531 , Issue.2 , pp. 109-114
    • Shav-Tal, Y.1    Zipori, D.2
  • 20
    • 0035242433 scopus 로고    scopus 로고
    • An RNA recognition motif (RRM) is required for the localization of PTB-associated splicing factor (PSF) to subnuclear speckles
    • Dye BT, Patton JG. An RNA recognition motif (RRM) is required for the localization of PTB-associated splicing factor (PSF) to subnuclear speckles. Exp Cell Res 2001; 263:131-144
    • (2001) Exp Cell Res , vol.263 , pp. 131-144
    • Dye, B.T.1    Patton, J.G.2
  • 21
    • 38049153326 scopus 로고    scopus 로고
    • The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha
    • Buxadé M, Morrice N, Krebs DL, Proud CG. The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha. J Biol Chem 2008; 283:57-65.
    • (2008) J Biol Chem , vol.283 , pp. 57-65
    • Buxadé, M.1    Morrice, N.2    Krebs, D.L.3    Proud, C.G.4
  • 23
    • 67349211222 scopus 로고    scopus 로고
    • BRK phosphorylates PSF promoting its cytoplasmic localization and cell cycle arrest
    • Lukong KE, Huot ME, Richard S. BRK phosphorylates PSF promoting its cytoplasmic localization and cell cycle arrest. Cell Signal 2009; 21:1415-1422
    • (2009) Cell Signal , vol.21 , pp. 1415-1422
    • Lukong, K.E.1    Huot, M.E.2    Richard, S.3
  • 24
    • 0347635470 scopus 로고    scopus 로고
    • Binding of mouse VL30 retrotransposon RNA to PSF protein induces genes repressed by PSF: Effects on steroidogenesis and oncogenesis
    • DOI 10.1073/pnas.0307794100
    • Song X, Sui A, Garen A. Binding of mouse VL30 retrotransposon RNA to PSF protein induces genes repressed by PSF: effects on steroidogenesis and oncogenesis. Proc Natl Acad Sci USA 2004; 101:621-626 (Pubitemid 38084686)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.2 , pp. 621-626
    • Song, X.1    Sui, A.2    Garen, A.3
  • 27
    • 0042284848 scopus 로고    scopus 로고
    • PSF-TFE3 oncoprotein in papillary renal cell carcinoma inactivates TFE3 and p53 through cytoplasmic sequestration
    • DOI 10.1038/sj.onc.1206643
    • Mathur M, Das S, Samuels HH. PSF-TFE3 oncoprotein in papillary renal cell carcinoma inactivates TFE3 and p53 through cytoplasmic sequestration. Oncogene 2003; 22:5031-5044 (Pubitemid 37026401)
    • (2003) Oncogene , vol.22 , Issue.32 , pp. 5031-5044
    • Mathur, M.1    Das, S.2    Samuels, H.H.3
  • 28
    • 48949100777 scopus 로고    scopus 로고
    • Proteomic identification of a PSF/p54nrb heterodimer as RNF43 oncoprotein-interacting proteins
    • Miyamoto K, Sakurai H, Sugiura T. Proteomic identification of a PSF/p54nrb heterodimer as RNF43 oncoprotein-interacting proteins. Proteomics 2008; 8:2907-2910
    • (2008) Proteomics , vol.8 , pp. 2907-2910
    • Miyamoto, K.1    Sakurai, H.2    Sugiura, T.3
  • 29
    • 85078509066 scopus 로고    scopus 로고
    • HuR in the mammalian genotoxic response
    • Gorospe M. HuR in the mammalian genotoxic response. Cell Cycle 2003; 2:412-414
    • (2003) Cell Cycle , vol.2 , pp. 412-414
    • Gorospe, M.1
  • 30
    • 34547651351 scopus 로고    scopus 로고
    • Posttranscriptional orchestration of an anti-apoptotic program by HuR
    • Abdelmohsen K, Lal A, Kim HH, Gorospe M. Posttranscriptional orchestration of an anti-apoptotic program by HuR. Cell Cycle 2007; 6:1288-1292 (Pubitemid 47327958)
    • (2007) Cell Cycle , vol.6 , Issue.11 , pp. 1288-1292
    • Abdelmohsen, K.1    Lal, A.2    Hyeon, H.K.3    Gorospe, M.4
  • 31
    • 55849099956 scopus 로고    scopus 로고
    • Modification at HuR (S242) alters HuR localization and proliferative influence
    • Kim HH, Yang X, Kuwano Y, Gorospe M. Modification at HuR (S242) alters HuR localization and proliferative influence. Cell Cycle 2008; 7:3371-3377
    • (2008) Cell Cycle , vol.7 , pp. 3371-3377
    • Kim, H.H.1    Yang, X.2    Kuwano, Y.3    Gorospe, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.