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Gene Review

Ctbp1  -  C-terminal binding protein 1

Rattus norvegicus

Synonyms: 50 kDa BFA-dependent ADP-ribosylation substrate, 50-kDaBFA-inducedADP-ribosylatedsubstrate, BARS-50, Bars, C-terminal-binding protein 1, ...
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High impact information on Ctbp1

  • CtBP/BARS induces fission of Golgi membranes by acylating lysophosphatidic acid [1].
  • Here we show that CtBP/BARS, a protein that functions in the dynamics of Golgi tubules, is an essential component of the fission machinery operating at Golgi tubular networks, including Golgi compartments involved in protein transport and sorting [1].
  • The further addition of extracts enriched in native BARS-50 abolished the ability of ADP-ribosylated cytosol to support the effect of BFA [2].
  • BARS-50 can bind GTP, as indicated by blot-overlay studies with [alpha-32P]GTP and by photoaffinity labeling with guanosine 5'-[gamma-32P] [beta,gamma-(4-azidoanilido)]triphosphate [3].
  • CtBP (carboxyl-terminal binding protein) has been shown to be a highly conserved co-repressor of transcription that is important in development, cell cycle regulation, and transformation [4].

Biological context of Ctbp1

  • We found that the protein CtBP3/BARS (BARS) was responsible for driving the fission of Golgi membranes during mitosis in vivo [5].
  • We find that CtBP/BARS uses acyl-CoA to selectively catalyse the acylation of lysophosphatidic acid to phosphatidic acid both in pure lipidic systems and in Golgi membranes, and that this reaction is essential for fission [1].
  • These proteins have been identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and a novel guanine nucleotide binding protein (BARS-50), respectively [6].

Anatomical context of Ctbp1

  • The crystal structure together with the site-directed mutagenesis data and binding experiments suggest a rationale for the molecular mechanisms underlying the two fundamental co-existing, but diverse, activities supported by CtBP/BARS in the nucleus and in Golgi membranes [7].
  • We report that the 50-kDa BFA-induced ADP-ribosylated substrate (BARS-50) has native forms of 170 and 130 kDa, as determined by gel filtration of rat brain cytosol, indicating that BARS-50 might exist as a multimeric complex [3].
  • Interaction with CtBP was shown to be important in the repression of transcription by EBNA3A and in the ability of EBNA3A to cooperate with activated Ras to immortalize and transform primary rat embryo fibroblasts [4].
  • The fissiogenic activity of CtBP3/BARS has a role in the fragmentation of the Golgi complex during mitosis and during intracellular membrane transport [8].

Associations of Ctbp1 with chemical compounds

  • Dicumarol, an inhibitor of ADP-ribosylation of CtBP3/BARS, fragments golgi non-compact tubular zones and inhibits intra-golgi transport [9].
  • The CtBP1-mediated repression was alleviated by trichostatin A treatment, indicating that the CtBP inhibitory mechanism is dependent on the activity of histone deacetylases [10].

Analytical, diagnostic and therapeutic context of Ctbp1


  1. CtBP/BARS induces fission of Golgi membranes by acylating lysophosphatidic acid. Weigert, R., Silletta, M.G., Spanò, S., Turacchio, G., Cericola, C., Colanzi, A., Senatore, S., Mancini, R., Polishchuk, E.V., Salmona, M., Facchiano, F., Burger, K.N., Mironov, A., Luini, A., Corda, D. Nature (1999) [Pubmed]
  2. Role of NAD+ and ADP-ribosylation in the maintenance of the Golgi structure. Mironov, A., Colanzi, A., Silletta, M.G., Fiucci, G., Flati, S., Fusella, A., Polishchuk, R., Mironov, A., Di Tullio, G., Weigert, R., Malhotra, V., Corda, D., De Matteis, M.A., Luini, A. J. Cell Biol. (1997) [Pubmed]
  3. Evidence that the 50-kDa substrate of brefeldin A-dependent ADP-ribosylation binds GTP and is modulated by the G-protein beta gamma subunit complex. Di Girolamo, M., Silletta, M.G., De Matteis, M.A., Braca, A., Colanzi, A., Pawlak, D., Rasenick, M.M., Luini, A., Corda, D. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  4. Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A cooperate to bind the co-repressor carboxyl-terminal-binding protein (CtBP). Hickabottom, M., Parker, G.A., Freemont, P., Crook, T., Allday, M.J. J. Biol. Chem. (2002) [Pubmed]
  5. Mitotic Golgi partitioning is driven by the membrane-fissioning protein CtBP3/BARS. Hidalgo Carcedo, C., Bonazzi, M., Spanò, S., Turacchio, G., Colanzi, A., Luini, A., Corda, D. Science (2004) [Pubmed]
  6. Role of brefeldin A-dependent ADP-ribosylation in the control of intracellular membrane transport. Silletta, M.G., Colanzi, A., Weigert, R., Di Girolamo, M., Santone, I., Fiucci, G., Mironov, A., De Matteis, M.A., Luini, A., Corda, D. Mol. Cell. Biochem. (1999) [Pubmed]
  7. CtBP/BARS: a dual-function protein involved in transcription co-repression and Golgi membrane fission. Nardini, M., Spanò, S., Cericola, C., Pesce, A., Massaro, A., Millo, E., Luini, A., Corda, D., Bolognesi, M. EMBO J. (2003) [Pubmed]
  8. Purification and functional properties of the membrane fissioning protein CtBP3/BARS. Valente, C., Spanò, S., Luini, A., Corda, D. Meth. Enzymol. (2005) [Pubmed]
  9. Dicumarol, an inhibitor of ADP-ribosylation of CtBP3/BARS, fragments golgi non-compact tubular zones and inhibits intra-golgi transport. Mironov, A.A., Colanzi, A., Polishchuk, R.S., Beznoussenko, G.V., Mironov, A.A., Fusella, A., Di Tullio, G., Silletta, M.G., Corda, D., De Matteis, M.A., Luini, A. Eur. J. Cell Biol. (2004) [Pubmed]
  10. HMG box transcription factor TCF-4's interaction with CtBP1 controls the expression of the Wnt target Axin2/Conductin in human embryonic kidney cells. Valenta, T., Lukas, J., Korinek, V. Nucleic Acids Res. (2003) [Pubmed]
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