3 results on '"Cericola, Claudia"'
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2. The Golgi mitotic checkpoint is controlled by BARS-dependent fission of the Golgi ribbon into separate stacks in G2.
- Author
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Colanzi, Antonino, Carcedo, Cristina Hidalgo, Persico, Angela, Cericola, Claudia, Turacchio, Gabriele, Bonazzi, Matteo, Luini, Alberto, and Corda, Daniela
- Subjects
GOLGI apparatus ,ORGANELLES ,MITOSIS ,CELL cycle ,CELL division ,MOLECULAR biology - Abstract
The Golgi ribbon is a complex structure of many stacks interconnected by tubules that undergo fragmentation during mitosis through a multistage process that allows correct Golgi inheritance. The fissioning protein CtBP1-S/BARS (BARS) is essential for this, and is itself required for mitotic entry: a block in Golgi fragmentation results in cell-cycle arrest in G2, defining the ‘Golgi mitotic checkpoint’. Here, we clarify the precise stage of Golgi fragmentation required for mitotic entry and the role of BARS in this process. Thus, during G2, the Golgi ribbon is converted into isolated stacks by fission of interstack connecting tubules. This requires BARS and is sufficient for G2/M transition. Cells without a Golgi ribbon are independent of BARS for Golgi fragmentation and mitotic entrance. Remarkably, fibroblasts from BARS-knockout embryos have their Golgi complex divided into isolated stacks at all cell-cycle stages, bypassing the need for BARS for Golgi fragmentation. This identifies the precise stage of Golgi fragmentation and the role of BARS in the Golgi mitotic checkpoint, setting the stage for molecular analysis of this process. [ABSTRACT FROM AUTHOR]
- Published
- 2007
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3. Molecular mechanism and functional role of brefeldin A-mediated ADP-ribosylation of CtBP1/BARS
- Author
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Andrea Urbani, Claudia Cericola, Daniela Corda, Andrea R. Beccari, Maurizio Ronci, Prisca Liberali, Marco Nardini, Martino Bolognesi, Vasiliki S. Lalioti, Giuliana Catara, Carmen Valente, Agostino Bruno, Antonino Colanzi, Antonio De Flora, Alberto Luini, Giovanna Grimaldi, National Institutes of Health (US), Associazione Italiana per la Ricerca sul Cancro, Colanzi, Antonino, Grimaldi, Giovanna, Catara, Giuliana, Valente, Carmen, Cericola, Claudia, Liberali, Prisca, Ronci, Maurizio, Lalioti, Vasiliki S, Bruno, Agostino, Beccari, Andrea R, Urbani, Andrea, De Flora, Antonio, Nardini, Marco, Bolognesi, Martino, Luini, Alberto, and Corda, Daniela
- Subjects
Models, Molecular ,anticancer molecules ,chemistry.chemical_compound ,Cytosol ,Membrane fission ,Competitive ,Models ,Multidisciplinary ,Membrane Glycoproteins ,Blotting ,Settore BIO/12 ,Cell cycle ,Brefeldin A ,Biological Sciences ,Cell biology ,DNA-Binding Proteins ,ADP-ribosylation ,symbols ,mitosis ,Animals ,HeLa Cells ,Humans ,Protein Processing, Post-Translational ,Alcohol Oxidoreductases ,Antigens, CD38 ,Protein Binding ,Binding Sites ,Rats ,ADP-ribosyl Cyclase ,Blotting, Western ,NAD ,cell signaling ,Golgi fragmentation ,Binding, Competitive ,Protein Structure, Tertiary ,Adenosine Diphosphate Ribose ,Western ,Intracellular ,Protein Structure ,Biology ,symbols.namesake ,Antigens ,Mitosis ,Protein Processing ,Post-Translational ,Molecular ,Golgi apparatus ,Binding ,ADP-ribosyl Cyclase 1 ,chemistry ,CD38 ,Tertiary - Abstract
ADP-ribosylation is a posttranslational modification that modulates the functions of many target proteins. We previously showed that the fungal toxin brefeldin A (BFA) induces the ADP-ribosylation of C-terminal-binding protein-1 short-form/BFA-ADP-ribosylation substrate (CtBP1-S/BARS), a bifunctional protein with roles in the nucleus as a transcription factor and in the cytosol as a regulator of membrane fission during intracellular trafficking and mitotic partitioning of the Golgi complex. Here, we report that ADP-ribosylation of CtBP1-S/BARS by BFA occurs via a nonconventional mechanism that comprises two steps: (i) synthesis of a BFA-ADP-ribose conjugate by the ADP-ribosyl cyclase CD38 and (ii) covalent binding of the BFA-ADP-ribose conjugate into the CtBP1-S/BARS NAD+-binding pocket. This results in the locking of CtBP1-S/BARS in a dimeric conformation, which prevents its binding to interactors known to be involved in membrane fission and, hence, in the inhibition of the fission machinery involved in mitotic Golgi partitioning. As this inhibition may lead to arrest of the cell cycle in G2, these findings provide a strategy for the design of pharmacological blockers of cell cycle in tumor cells that express high levels of CD38., We thank all colleagues who kindly provided antibodies and reagents; Dr. J. Donaldson (National Institutes of Health) for BFA analogs; Dr. C. P. Berrie for editorial assistance; and Drs. C. Limina, A. Tamburro, M. G. Silletta, R. Weigert, and S. Spanò (Negri Sud Institute) for performing initial experiments. We also acknowledge financial support from Italian Association for Cancer Research (AIRC) through the Grants IG4664 and IG10341 (to D.C.), IG4700 (to A.L.), and IG6074 (to A.C.); and from the Liguria Region and the Ministry of Education, University, and Research (Fund for Investments in Basic Research Project; A.D.F.). G.G. and C.V. received fellowships from AIRC (Italian Foundation for Cancer Research). Financial support from Technological Innovation Fund DM 24/09/2009, Legge 46/82-MEF, and Project FaReBio di Qualità also is acknowledged
- Published
- 2013
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