메뉴 건너뛰기




Volumn 22, Issue 12, 2003, Pages 3122-3130

CtBP/BARS: A dual-function protein involved in transcription co-repression and Golgi membrane fission

Author keywords

Acyl CoA; Brefeldin A; Golgi membrane; NAD; Transcription co repression

Indexed keywords

ACYL COENZYME A; ADENOSINE DIPHOSPHATE; BINDING PROTEIN; BREFELDIN A ADENOSINE DIPHOSPHATE RIBOSYL SUBSTRATE; C TERMINAL BINDING PROTEIN; DNA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 0037938505     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg283     Document Type: Article
Times cited : (136)

References (38)
  • 1
    • 0028865843 scopus 로고
    • 3D Domain swapping: A mechanism for oligomer assembly
    • Bennett, M.J., Schlunegger, M.P. and Eisenberg, D. (1995) 3D Domain swapping: a mechanism for oligomer assembly. Protein Sci., 4, 2455-2468.
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 3
    • 0027509346 scopus 로고
    • A region in the C-terminus of adenovirus 2/5 E1a protein is required for association with a cellular phosphoprotein and important for the negative modulation of T24-ras mediated transformation, tumorigenesis and metastasis
    • Boyd, J.M., Subramanian, T., Schaeper, U., La Regina, M., Bayley, S. and Chinnadurai, G. (1993) A region in the C-terminus of adenovirus 2/5 E1a protein is required for association with a cellular phosphoprotein and important for the negative modulation of T24-ras mediated transformation, tumorigenesis and metastasis. EMBO J., 12, 469-478.
    • (1993) EMBO J. , vol.12 , pp. 469-478
    • Boyd, J.M.1    Subramanian, T.2    Schaeper, U.3    La Regina, M.4    Bayley, S.5    Chinnadurai, G.6
  • 4
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. (1998) Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D, 54, 905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 5
    • 0030893657 scopus 로고    scopus 로고
    • NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding
    • Carugo, O. and Argos, P. (1997) NADP-dependent enzymes. I: conserved stereochemistry of cofactor binding. Proteins, 28, 10-28.
    • (1997) Proteins , vol.28 , pp. 10-28
    • Carugo, O.1    Argos, P.2
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4. (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D, 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 8
    • 0033564261 scopus 로고    scopus 로고
    • Net, a negative Ras-switchable TCF, contains a second inhibition domain, the CID, that mediates repression through interactions with CtBP and de-acetylation
    • Criqui-Filipe, P., Ducret, C., Maira, S.M. and Wasylyk, B. (1999) Net, a negative Ras-switchable TCF, contains a second inhibition domain, the CID, that mediates repression through interactions with CtBP and de-acetylation. EMBO J., 18, 3392-3403.
    • (1999) EMBO J. , vol.18 , pp. 3392-3403
    • Criqui-Filipe, P.1    Ducret, C.2    Maira, S.M.3    Wasylyk, B.4
  • 9
    • 0028014643 scopus 로고
    • Stimulation of endogenous ADP-ribosylation by brefeldin A
    • De Matteis, M.A. et al. (1994) Stimulation of endogenous ADP-ribosylation by brefeldin A. Proc. Natl Acad. Sci. USA, 91, 1114-1118.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1114-1118
    • De Matteis, M.A.1
  • 11
    • 0029125678 scopus 로고
    • Evidence that the 50 kDa substrate of brefeldin A-dependent ADP-ribosylation binds GTP and is modulated by the G-protein βγ subunit complex
    • Di Girolamo, M., Silletta, M.G., De Matteis, M.A., Braca, A., Colanzi, A., Pawlak, D., Luini, A. and Corda, D. (1995) Evidence that the 50 kDa substrate of brefeldin A-dependent ADP-ribosylation binds GTP and is modulated by the G-protein βγ subunit complex. Proc. Natl Acad. Sci. USA, 92, 7065-7069.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7065-7069
    • Di Girolamo, M.1    Silletta, M.G.2    De Matteis, M.A.3    Braca, A.4    Colanzi, A.5    Pawlak, D.6    Luini, A.7    Corda, D.8
  • 12
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R.A. and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A, 47, 392-400.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 13
    • 0028278602 scopus 로고
    • Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 Å resolution
    • Goldberg, J.D., Yoshida, T. and Brick, P. (1994) Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4 Å resolution. J. Mol. Biol., 236, 1123-1140.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1123-1140
    • Goldberg, J.D.1    Yoshida, T.2    Brick, P.3
  • 14
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 15
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 18
    • 0000243829 scopus 로고
    • PROCHECK, a program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S. and Thornton, J.M. (1993) PROCHECK, a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 19
    • 0036850942 scopus 로고    scopus 로고
    • Dehydrogenases, NAD and transcription. What's the connection?
    • Marmorstein, R. (2002) Dehydrogenases, NAD and transcription. What's the connection? Structure, 10, 1465-1466.
    • (2002) Structure , vol.10 , pp. 1465-1466
    • Marmorstein, R.1
  • 20
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt, E.A. and Murphy, M.E.P. (1994) Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallogr. D, 50, 869-873.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 21
    • 0030827627 scopus 로고    scopus 로고
    • + and ADP-ribosylation in the maintenance of the Golgi structure
    • + and ADP-ribosylation in the maintenance of the Golgi structure. J. Cell Biol., 139, 1109-1118.
    • (1997) J. Cell Biol. , vol.139 , pp. 1109-1118
    • Mironov, A.1
  • 22
  • 23
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinoski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol., 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinoski, Z.1    Minor, W.2
  • 25
    • 0015834475 scopus 로고
    • Comparison of super-secondary structures in proteins
    • Rao, S.T. and Rossmann, M.G. (1973) Comparison of super-secondary structures in proteins. J. Mol. Biol., 76, 241-256.
    • (1973) J. Mol. Biol. , vol.76 , pp. 241-256
    • Rao, S.T.1    Rossmann, M.G.2
  • 26
    • 0028838348 scopus 로고
    • Molecular cloning and characterization of a cellular phosphoprotein that interacts with a conserved C-terminal domain of adenovirus E1A involved in negative modulation of oncogenic transformation
    • Schaeper, U., Boyd, J.M., Verma, S., Uhlmann, E., Subramanian, T. and Chinnadurai, G. (1995) Molecular cloning and characterization of a cellular phosphoprotein that interacts with a conserved C-terminal domain of adenovirus E1A involved in negative modulation of oncogenic transformation. Proc. Natl Acad. Sci. USA, 92, 10467-10471.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10467-10471
    • Schaeper, U.1    Boyd, J.M.2    Verma, S.3    Uhlmann, E.4    Subramanian, T.5    Chinnadurai, G.6
  • 28
    • 0029901451 scopus 로고    scopus 로고
    • The CtBP binding domain in the adenovirus E1A protein controls CRI-dependent transactivation
    • Sollerbrant, K., Chinnadurai, G., Svensson, C. (1996) The CtBP binding domain in the adenovirus E1A protein controls CRI-dependent transactivation. Nucleic Acids Res., 24, 2578-2584.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2578-2584
    • Sollerbrant, K.1    Chinnadurai, G.2    Svensson, C.3
  • 29
    • 0033580845 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of brefeldin A-ADP-ribosylated substrate
    • Spanò, S. et al. (1999) Molecular cloning and functional characterization of brefeldin A-ADP-ribosylated substrate. J. Biol. Chem., 274, 17705-17710.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17705-17710
    • Spanò, S.1
  • 30
    • 0030584680 scopus 로고    scopus 로고
    • Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase
    • Stoll, V.S, Kimber, M.S. and Pai, E.F. (1996) Insights into substrate binding by D-2-ketoacid dehydrogenases from the structure of Lactobacillus pentosus D-lactate dehydrogenase. Structure, 4, 437-447.
    • (1996) Structure , vol.4 , pp. 437-447
    • Stoll, V.S.1    Kimber, M.S.2    Pai, E.F.3
  • 31
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for MIR and MAD
    • Terwilliger, T.C. and Berendzen, J. (1999) Automated structure solution for MIR and MAD. Acta Crystallogr. D, 55, 849-861.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 32
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 33
    • 0032167456 scopus 로고    scopus 로고
    • Cloning and characterization of mCtBP2, a co-repressor that associates with basic Krüppel-like factor and other mammalian transcriptional regulators
    • Turner, J. and Crossley, M. (1998) Cloning and characterization of mCtBP2, a co-repressor that associates with basic Krüppel-like factor and other mammalian transcriptional regulators. EMBO J., 17, 5129-5140.
    • (1998) EMBO J. , vol.17 , pp. 5129-5140
    • Turner, J.1    Crossley, M.2
  • 34
    • 0034865435 scopus 로고    scopus 로고
    • The CtBP family: Enigmatic and enzymatic transcriptional co-repressors
    • Turner, J. and Crossley, M. (2001) The CtBP family: enigmatic and enzymatic transcriptional co-repressors. BioEssays, 23, 683-690.
    • (2001) BioEssays , vol.23 , pp. 683-690
    • Turner, J.1    Crossley, M.2
  • 35
    • 0033082065 scopus 로고    scopus 로고
    • Optimizing Shake-and-Bake for proteins
    • Weeks, C.M. and Miller, R. (1999) Optimizing Shake-and-Bake for proteins. Acta Crystallogr. D, 55, 492-500.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 492-500
    • Weeks, C.M.1    Miller, R.2
  • 36
    • 0033604565 scopus 로고    scopus 로고
    • CtBP/BARS induces fission of Golgi membranes by acylating lysophosphatidic acid
    • Weigert, R. et al. (1999) CtBP/BARS induces fission of Golgi membranes by acylating lysophosphatidic acid. Nature, 402, 429-433.
    • (1999) Nature , vol.402 , pp. 429-433
    • Weigert, R.1
  • 38
    • 0037040581 scopus 로고    scopus 로고
    • Regulation of corepressor function by nuclear NADH
    • Zhang, Q., Piston, D.W. and Goodman, R.H. (2002) Regulation of corepressor function by nuclear NADH. Science, 295, 1895-1897.
    • (2002) Science , vol.295 , pp. 1895-1897
    • Zhang, Q.1    Piston, D.W.2    Goodman, R.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.