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Start Over Author "Cericola, Claudia" Topic golgi apparatus
4 results on '"Cericola, Claudia"'

1. The Golgi mitotic checkpoint is controlled by BARS-dependent fission of the Golgi ribbon into separate stacks in G2.

Author

Colanzi A, Hidalgo Carcedo C, Persico A, Cericola C, Turacchio G, Bonazzi M, Luini A, and Corda D

Subjects
Alcohol Oxidoreductases genetics, DNA-Binding Proteins genetics, Fluorescence Recovery After Photobleaching, Golgi Apparatus ultrastructure, Green Fluorescent Proteins metabolism, HeLa Cells, Humans, Alcohol Oxidoreductases metabolism, DNA-Binding Proteins metabolism, G2 Phase, Golgi Apparatus physiology, Mitosis
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.

Published
2007
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2. CtBP/BARS: a dual-function protein involved in transcription co-repression and Golgi membrane fission.

Author

Nardini M, Spanò S, Cericola C, Pesce A, Massaro A, Millo E, Luini A, Corda D, and Bolognesi M

Subjects
Acyl Coenzyme A metabolism, Amino Acid Sequence, Animals, Binding Sites, Carrier Proteins genetics, Carrier Proteins metabolism, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, NAD chemistry, NAD metabolism, Peptides chemistry, Peptides metabolism, Protein Binding, Protein Folding, Protein Structure, Tertiary, Rats, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins metabolism, Repressor Proteins genetics, Repressor Proteins metabolism, Sequence Alignment, Carrier Proteins chemistry, Cell Membrane metabolism, Golgi Apparatus metabolism, Repressor Proteins chemistry, Transcription Factors, Transcription, Genetic
Abstract

C-terminal-binding protein/brefeldin A-ADP ribosylated substrate (CtBP/BARS) plays key roles in development and oncogenesis as a transcription co-repressor, and in intracellular traffic as a promoter of Golgi membrane fission. Co-repressor activity is regulated by NAD(H) binding to CtBP/BARS, while membrane fission is associated with its acyl-CoA-dependent acyltransferase activity. Here, we report the crystal structures of rat CtBP/BARS in a binary complex with NAD(H), and in a ternary complex with a PIDLSKK peptide mimicking the consensus motif (PXDLS) recognized in CtBP/BARS cellular partners. The structural data show CtBP/BARS in a NAD(H)-bound dimeric form; the peptide binding maps the recognition site for DNA-binding proteins and histone deacetylases to an N-terminal region of the protein. 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.

Published
2003
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4. Molecular mechanism and functional role of brefeldin A-mediated ADP-ribosylation of CtBP1/BARS

Author

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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