메뉴 건너뛰기




Volumn 3, Issue 5, 2013, Pages 1526-1538

RhoGAPs Attenuate Cell Proliferation by Direct Interaction with p53 Tetramerization Domain

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN ARHGAP11A; PROTEIN P53; PROTEIN P63; PROTEIN P73; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG; DNA; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PROTEIN BINDING; RHO GTPASE-ACTIVATING PROTEIN; RHO GTPASE-ACTIVATING PROTEIN 15, HUMAN; SMALL INTERFERING RNA;

EID: 84878603920     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2013.04.017     Document Type: Article
Times cited : (57)

References (40)
  • 1
    • 80455168319 scopus 로고    scopus 로고
    • Quaternary structure of the specific p53-DNA complex reveals the mechanism of p53 mutant dominance
    • Aramayo R., Sherman M.B., Brownless K., Lurz R., Okorokov A.L., Orlova E.V. Quaternary structure of the specific p53-DNA complex reveals the mechanism of p53 mutant dominance. Nucleic Acids Res. 2011, 39:8960-8971.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 8960-8971
    • Aramayo, R.1    Sherman, M.B.2    Brownless, K.3    Lurz, R.4    Okorokov, A.L.5    Orlova, E.V.6
  • 2
    • 78649466451 scopus 로고    scopus 로고
    • Cancer: the blind spot of p53
    • Berns A. Cancer: the blind spot of p53. Nature 2010, 468:519-520.
    • (2010) Nature , vol.468 , pp. 519-520
    • Berns, A.1
  • 3
    • 19444387096 scopus 로고    scopus 로고
    • RASA1: variable phenotype with capillary and arteriovenous malformations
    • Boon L.M., Mulliken J.B., Vikkula M. RASA1: variable phenotype with capillary and arteriovenous malformations. Curr. Opin. Genet. Dev. 2005, 15:265-269.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 265-269
    • Boon, L.M.1    Mulliken, J.B.2    Vikkula, M.3
  • 4
    • 74549130412 scopus 로고    scopus 로고
    • Conservation of DNA-binding specificity and oligomerisation properties within the p53 family
    • Brandt T., Petrovich M., Joerger A.C., Veprintsev D.B. Conservation of DNA-binding specificity and oligomerisation properties within the p53 family. BMC Genomics 2009, 10:628.
    • (2009) BMC Genomics , vol.10 , pp. 628
    • Brandt, T.1    Petrovich, M.2    Joerger, A.C.3    Veprintsev, D.B.4
  • 5
    • 80053064491 scopus 로고    scopus 로고
    • The impact of acetylation and deacetylation on the p53 pathway
    • Brooks C.L., Gu W. The impact of acetylation and deacetylation on the p53 pathway. Protein Cell 2011, 2:456-462.
    • (2011) Protein Cell , vol.2 , pp. 456-462
    • Brooks, C.L.1    Gu, W.2
  • 8
    • 0037855764 scopus 로고    scopus 로고
    • Deleted in liver cancer (DLC) 2 encodes a RhoGAP protein with growth suppressor function and is underexpressed in hepatocellular carcinoma
    • Ching Y.P., Wong C.M., Chan S.F., Leung T.H., Ng D.C., Jin D.Y., Ng I.O. Deleted in liver cancer (DLC) 2 encodes a RhoGAP protein with growth suppressor function and is underexpressed in hepatocellular carcinoma. J.Biol. Chem. 2003, 278:10824-10830.
    • (2003) J.Biol. Chem. , vol.278 , pp. 10824-10830
    • Ching, Y.P.1    Wong, C.M.2    Chan, S.F.3    Leung, T.H.4    Ng, D.C.5    Jin, D.Y.6    Ng, I.O.7
  • 10
    • 0032490855 scopus 로고    scopus 로고
    • Characterization of the oligomerization defects of two p53 mutants found in families with Li-Fraumeni and Li-Fraumeni-like syndrome
    • Davison T.S., Yin P., Nie E., Kay C., Arrowsmith C.H. Characterization of the oligomerization defects of two p53 mutants found in families with Li-Fraumeni and Li-Fraumeni-like syndrome. Oncogene 1998, 17:651-656.
    • (1998) Oncogene , vol.17 , pp. 651-656
    • Davison, T.S.1    Yin, P.2    Nie, E.3    Kay, C.4    Arrowsmith, C.H.5
  • 12
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville S., Hall A. Rho GTPases in cell biology. Nature 2002, 420:629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 13
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla A.M., Rousseau F., Schymkowitz J., Serrano L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nat. Biotechnol. 2004, 22:1302-1306.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 15
    • 5044228029 scopus 로고    scopus 로고
    • Genetic predisposition to cancer-insights from population genetics
    • Frank S.A. Genetic predisposition to cancer-insights from population genetics. Nat. Rev. Genet. 2004, 5:764-772.
    • (2004) Nat. Rev. Genet. , vol.5 , pp. 764-772
    • Frank, S.A.1
  • 16
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations
    • Guerois R., Nielsen J.E., Serrano L. Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. J.Mol. Biol. 2002, 320:369-387.
    • (2002) J.Mol. Biol. , vol.320 , pp. 369-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3
  • 17
    • 14944378159 scopus 로고    scopus 로고
    • Redox factor 1 (Ref-1) enhances specific DNA binding of p53 by promoting p53 tetramerization
    • Hanson S., Kim E., Deppert W. Redox factor 1 (Ref-1) enhances specific DNA binding of p53 by promoting p53 tetramerization. Oncogene 2005, 24:1641-1647.
    • (2005) Oncogene , vol.24 , pp. 1641-1647
    • Hanson, S.1    Kim, E.2    Deppert, W.3
  • 18
    • 43049120043 scopus 로고    scopus 로고
    • A comprehensive analysis of transcript signatures of the phosphatidylinositol-3 kinase/protein kinase B signal-transduction pathway in prostate cancer
    • Hellwinkel O.J., Rogmann J.P., Asong L.E., Luebke A.M., Eichelberg C., Ahyai S., Isbarn H., Graefen M., Huland H., Schlomm T. A comprehensive analysis of transcript signatures of the phosphatidylinositol-3 kinase/protein kinase B signal-transduction pathway in prostate cancer. BJU Int. 2008, 101:1454-1460.
    • (2008) BJU Int. , vol.101 , pp. 1454-1460
    • Hellwinkel, O.J.1    Rogmann, J.P.2    Asong, L.E.3    Luebke, A.M.4    Eichelberg, C.5    Ahyai, S.6    Isbarn, H.7    Graefen, M.8    Huland, H.9    Schlomm, T.10
  • 19
    • 79955661909 scopus 로고    scopus 로고
    • Expression analysis of genes located in the minimally deleted regions of 13q14 and 11q22-23 in chronic lymphocytic leukemia-unexpected expression pattern of the RHO GTPase activator ARHGAP20
    • Herold T., Jurinovic V., Mulaw M., Seiler T., Dufour A., Schneider S., Kakadia P.M., Feuring-Buske M., Braess J., Spiekermann K., et al. Expression analysis of genes located in the minimally deleted regions of 13q14 and 11q22-23 in chronic lymphocytic leukemia-unexpected expression pattern of the RHO GTPase activator ARHGAP20. Genes Chromosomes Cancer 2011, 50:546-558.
    • (2011) Genes Chromosomes Cancer , vol.50 , pp. 546-558
    • Herold, T.1    Jurinovic, V.2    Mulaw, M.3    Seiler, T.4    Dufour, A.5    Schneider, S.6    Kakadia, P.M.7    Feuring-Buske, M.8    Braess, J.9    Spiekermann, K.10
  • 20
    • 33645769516 scopus 로고    scopus 로고
    • Comparative and evolutionary analysis of genes encoding small GTPases and their activating proteins in eukaryotic genomes
    • Jiang S.Y., Ramachandran S. Comparative and evolutionary analysis of genes encoding small GTPases and their activating proteins in eukaryotic genomes. Physiol. Genomics 2006, 24:235-251.
    • (2006) Physiol. Genomics , vol.24 , pp. 235-251
    • Jiang, S.Y.1    Ramachandran, S.2
  • 21
    • 3242763031 scopus 로고    scopus 로고
    • ARHGAP8 is a novel member of the RHOGAP family related to ARHGAP1/CDC42GAP/p50RHOGAP: mutation and expression analyses in colorectal and breast cancers
    • Johnstone C.N., Castellví-Bel S., Chang L.M., Bessa X., Nakagawa H., Harada H., Sung R.K., Piqué J.M., Castells A., Rustgi A.K. ARHGAP8 is a novel member of the RHOGAP family related to ARHGAP1/CDC42GAP/p50RHOGAP: mutation and expression analyses in colorectal and breast cancers. Gene 2004, 336:59-71.
    • (2004) Gene , vol.336 , pp. 59-71
    • Johnstone, C.N.1    Castellví-Bel, S.2    Chang, L.M.3    Bessa, X.4    Nakagawa, H.5    Harada, H.6    Sung, R.K.7    Piqué, J.M.8    Castells, A.9    Rustgi, A.K.10
  • 22
    • 33747293858 scopus 로고    scopus 로고
    • Rho GTPase activating proteins in cancer phenotypes
    • Kandpal R.P. Rho GTPase activating proteins in cancer phenotypes. Curr. Protein Pept. Sci. 2006, 7:355-365.
    • (2006) Curr. Protein Pept. Sci. , vol.7 , pp. 355-365
    • Kandpal, R.P.1
  • 23
    • 0029044606 scopus 로고
    • MDM2 protein confers the resistance of a human glioblastoma cell line to cisplatin-induced apoptosis
    • Kondo S., Barnett G.H., Hara H., Morimura T., Takeuchi J. MDM2 protein confers the resistance of a human glioblastoma cell line to cisplatin-induced apoptosis. Oncogene 1995, 10:2001-2006.
    • (1995) Oncogene , vol.10 , pp. 2001-2006
    • Kondo, S.1    Barnett, G.H.2    Hara, H.3    Morimura, T.4    Takeuchi, J.5
  • 24
    • 40149083557 scopus 로고    scopus 로고
    • Deleted in liver cancer-1 (DLC-1): a tumor suppressor not just for liver
    • Liao Y.C., Lo S.H. Deleted in liver cancer-1 (DLC-1): a tumor suppressor not just for liver. Int. J. Biochem. Cell Biol. 2008, 40:843-847.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 843-847
    • Liao, Y.C.1    Lo, S.H.2
  • 25
    • 79952690543 scopus 로고    scopus 로고
    • How phosphorylation controls p53
    • MacLaine N.J., Hupp T.R. How phosphorylation controls p53. Cell Cycle 2011, 10:916-921.
    • (2011) Cell Cycle , vol.10 , pp. 916-921
    • MacLaine, N.J.1    Hupp, T.R.2
  • 27
    • 0032525133 scopus 로고    scopus 로고
    • Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain
    • Mateu M.G., Fersht A.R. Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain. EMBO J. 1998, 17:2748-2758.
    • (1998) EMBO J. , vol.17 , pp. 2748-2758
    • Mateu, M.G.1    Fersht, A.R.2
  • 28
    • 0031762533 scopus 로고    scopus 로고
    • Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP
    • Nassar N., Hoffman G.R., Manor D., Clardy J.C., Cerione R.A. Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP. Nat. Struct. Biol. 1998, 5:1047-1052.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1047-1052
    • Nassar, N.1    Hoffman, G.R.2    Manor, D.3    Clardy, J.C.4    Cerione, R.A.5
  • 29
    • 0033985661 scopus 로고    scopus 로고
    • Stimulation of p53 DNA binding by c-Abl requires the p53 C terminus and tetramerization
    • Nie Y., Li H.H., Bula C.M., Liu X. Stimulation of p53 DNA binding by c-Abl requires the p53 C terminus and tetramerization. Mol. Cell. Biol. 2000, 20:741-748.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 741-748
    • Nie, Y.1    Li, H.H.2    Bula, C.M.3    Liu, X.4
  • 30
    • 84867449930 scopus 로고    scopus 로고
    • Molecular markers for cancer prognosis and treatment: have we struck gold?
    • Nowsheen S., Aziz K., Panayiotidis M.I., Georgakilas A.G. Molecular markers for cancer prognosis and treatment: have we struck gold?. Cancer Lett. 2012, 327:142-152.
    • (2012) Cancer Lett. , vol.327 , pp. 142-152
    • Nowsheen, S.1    Aziz, K.2    Panayiotidis, M.I.3    Georgakilas, A.G.4
  • 33
    • 0033767235 scopus 로고    scopus 로고
    • Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation
    • Rodriguez M.S., Desterro J.M., Lain S., Lane D.P., Hay R.T. Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation. Mol. Cell. Biol. 2000, 20:8458-8467.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8458-8467
    • Rodriguez, M.S.1    Desterro, J.M.2    Lain, S.3    Lane, D.P.4    Hay, R.T.5
  • 34
    • 0037468639 scopus 로고    scopus 로고
    • ArhGAP15, a novel human RacGAP protein with GTPase binding property
    • Seoh M.L., Ng C.H., Yong J., Lim L., Leung T. ArhGAP15, a novel human RacGAP protein with GTPase binding property. FEBS Lett. 2003, 539:131-137.
    • (2003) FEBS Lett. , vol.539 , pp. 131-137
    • Seoh, M.L.1    Ng, C.H.2    Yong, J.3    Lim, L.4    Leung, T.5
  • 36
    • 0033930032 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis and mass spectrometry identification of proteins bound by a murine monoclonal anti-cardiolipin antibody: a powerful technique to characterize the cross-reactivity of a single autoantibody
    • Thebault S., Gilbert D., Machour N., Marvin L., Lange C., Tron F., Charlionet R. Two-dimensional electrophoresis and mass spectrometry identification of proteins bound by a murine monoclonal anti-cardiolipin antibody: a powerful technique to characterize the cross-reactivity of a single autoantibody. Electrophoresis 2000, 21:2531-2539.
    • (2000) Electrophoresis , vol.21 , pp. 2531-2539
    • Thebault, S.1    Gilbert, D.2    Machour, N.3    Marvin, L.4    Lange, C.5    Tron, F.6    Charlionet, R.7
  • 38
    • 33747840389 scopus 로고    scopus 로고
    • GRAMM-X public web server forprotein-protein docking
    • Tovchigrechko A., Vakser I.A. GRAMM-X public web server forprotein-protein docking. Nucleic Acids Res. 2006, 34(Web Server issue):W310-W314.
    • (2006) Nucleic Acids Res. , vol.34 , Issue.WEB SERVER ISSUE
    • Tovchigrechko, A.1    Vakser, I.A.2
  • 39
    • 34447537796 scopus 로고    scopus 로고
    • Irradiation-induced G2/M checkpoint response requires ERK1/2 activation
    • Yan Y., Black C.P., Cowan K.H. Irradiation-induced G2/M checkpoint response requires ERK1/2 activation. Oncogene 2007, 26:4689-4698.
    • (2007) Oncogene , vol.26 , pp. 4689-4698
    • Yan, Y.1    Black, C.P.2    Cowan, K.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.