Abstract
CtBP3/BARS was the third protein of the CtBP (C-terminal binding protein) family to be identified. It was initially isolated as a 50-kDa cytosolic protein during the characterisation of the molecular targets of the toxin brefeldin A (BFA). As this protein is a substrate of BFA-dependent ADP-ribosylation, it was initially named BARS-50 (BFA-dependent ADP-ribosylation substrate), or BARS. After its purification and cloning, the protein was shown to be the third member (hence CtBP3/BARS) of the CtBP transcription corepressor family of proteins, sharing a high degree of aminoacid identity with CtBPl (97%). CtBP3/BARS induces membrane fission in isolated Golgi membranes and is necessary for the fragmentation of the Golgi complex that occurs at the beginning of mitosis; its direct role in transcription regulation has not yet been specifically investigated. The CtBPs are thus a multifunctional protein family that can modulate both nuclear and cytosolic functions.
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Spanò, S., Carcedo, C.H., Corda, D. (2007). CtBP 3/BARS and Membrane Fission. In: GtBP Family Proteins. Molecular Biology Intelligence Unit. Springer, New York, NY. https://doi.org/10.1007/978-0-387-39973-7_10
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DOI: https://doi.org/10.1007/978-0-387-39973-7_10
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