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Your search keyword '"Piatti, S."' showing total 4 results
Start Over Author "Piatti, S." Publisher rockefeller institute press
4 results on '"Piatti, S."'

1. The beta4 integrin interactor p27(BBP/eIF6) is an essential nuclear matrix protein involved in 60S ribosomal subunit assembly

Author

Sanvito, F, Piatti, S, Lucchini, G, Marchisio, PC, Biffo, S., VILLA, ANTONELLO, BOSSI, MARIO, Sanvito, F, Piatti, S, Villa, A, Bossi, M, Lucchini, G, Marchisio, P, and Biffo, S

Subjects
Base Sequence, Sequence Homology, Amino Acid, DNA Primer, Molecular Sequence Data, Antigens, Nuclear, Saccharomyces cerevisiae, Recombinant Protein, Mitosi, Immunohistochemistry, Ribosome, Ribosomal Protein, Intermediate Filament Protein, Microscopy, Electron, Cell Nucleolu, Eukaryotic Initiation Factor, Phosphoprotein, Amino Acid Sequence, Carrier Protein, Fluorescent Antibody Technique, Indirect, Saccharomyces cerevisiae Protein, Human, Nuclear Protein
Abstract

p27(BBP/eIF6) is an evolutionarily conserved protein that was originally identified as p27(BBP), an interactor of the cytoplasmic domain of integrin beta4 and, independently, as the putative translation initiation factor eIF6. To establish the in vivo function of p27(BBP/eIF6), its topographical distribution was investigated in mammalian cells and the effects of disrupting the corresponding gene was studied in the budding yeast, Saccharomyces cerevisiae. In epithelial cells containing beta4 integrin, p27(BBP/eIF6) is present in the cytoplasm and enriched at hemidesmosomes with a pattern similar to that of beta4 integrin. Surprisingly, in the absence and in the presence of the beta4 integrin subunit, p27(BBP/eIF6) is in the nucleolus and associated with the nuclear matrix. Deletion of the IIH S. cerevisiae gene, encoding the yeast p27(BBP/eIF6) homologue, is lethal, and depletion of the corresponding gene product is associated with a dramatic decrease of the level of free ribosomal 60S subunit. Furthermore, human p27(BBP/eIF6) can rescue the lethal effect of the iihDelta yeast mutation. The data obtained in vivo suggest an evolutionarily conserved function of p27(BBP/eIF6) in ribosome biogenesis or assembly rather than in translation. A further function related to the beta4 integrin subunit may have evolved specifically in higher eukaryotic cells.

Published
1999

2. The RSC chromatin-remodelling complex influences mitotic exit and adaptation to the spindle assembly checkpoint by controlling Cdc14 phosphatase

Author

Rossio, V, Galati, E, Ferrari, M, Pellicioli, A, Sutani, T, Shirahige, K, Lucchini, G, Piatti, S, ROSSIO, VALENTINA, GALATI, ELENA, LUCCHINI, GIOVANNA, PIATTI, SIMONETTA, Rossio, V, Galati, E, Ferrari, M, Pellicioli, A, Sutani, T, Shirahige, K, Lucchini, G, Piatti, S, ROSSIO, VALENTINA, GALATI, ELENA, LUCCHINI, GIOVANNA, and PIATTI, SIMONETTA

Abstract

Upon prolonged activation of the spindle assembly checkpoint (SAC) cells escape from mitosis through a mechanism called adaptation or mitotic slippage, which is thought to underlie the resistance of cancer cells to anti-mitotic drugs. We show that this mechanism in budding yeast this mechanism depends on known essential and non-essential regulators of mitotic exit, such as the FEAR pathway for the release of the Cdc14 phosphatase from the nucleolus in early anaphase. Moreover, the RSC chromatin-remodelling complex bound to its accessory subunit Rsc2 is involved in this process as a novel component of the FEAR pathway. We show that Rsc2 interacts physically with the polo kinase Cdc5, a major regulator of Cdc14, and is required for timely phosphorylation of the Cdc14 inhibitor Net1, which is important to free Cdc14 in the active form. Altogether, our data suggest that fine tuning regulators of mitotic exit play an important rolehave important functions during in mitotic progression ofin cells treated with microtubule poisons, and might be promising targets for cancer treatment.

Published
2010

3. Budding yeast PAK kinases regulate mitotic exit by two different mechanisms

Author

Chiroli, E, Fraschini, R, Beretta, A, Tonelli, M, Lucchini, G, Piatti, S, FRASCHINI, ROBERTA, TONELLI, MARIAGRAZIA, LUCCHINI, GIOVANNA, PIATTI, SIMONETTA, Chiroli, E, Fraschini, R, Beretta, A, Tonelli, M, Lucchini, G, Piatti, S, FRASCHINI, ROBERTA, TONELLI, MARIAGRAZIA, LUCCHINI, GIOVANNA, and PIATTI, SIMONETTA

Abstract

We report the characterization of the dominant-negative CLA4t allele of the budding yeast CLA4 gene, encoding a member of the PAK family of protein kinases, which, together with its homologue STE20, plays an essential role in promoting budding and cytokinesis. Overproduction of the Cla4t protein likely inhibits both endogenous Cla4 and Ste20 and causes a delay in the onset of anaphase that correlates with inactivation of Cdc20/APC-dependent proteolysis of both the cyclinB Clb2 and securin. Although the precise mechanism of APC inhibition by Cla4t remains to be elucidated, our results suggest that Cla4 and Ste20 may regulate the first wave of cyclinB proteolysis mediated by Cdc20/APC, which has been shown to be crucial for activation of the Mitotic Exit Network. We show that the Cdk1-inhibitory kinase Swe1 is required for the Cla4t-dependent delay in cell cycle progression, suggesting that it might be required to prevent full Cdc20/APC and MEN activation. In addition, inhibition of PAK kinases by Cla4t prevents mitotic exit also by a Swe1-independent mechanism impinging directly on the MEN activator Tem1

Published
2003

4. The RSC chromatin-remodelling complex influences mitotic exit and adaptation to the spindle assembly checkpoint by controlling Cdc14 phosphatase

Author

Matteo Ferrari, Katsuhiko Shirahige, Simonetta Piatti, Valentina Rossio, Elena Galati, Achille Pellicioli, Takashi Sutani, Giovanna Lucchini, Rossio, V, Galati, E, Ferrari, M, Pellicioli, A, Sutani, T, Shirahige, K, Lucchini, G, and Piatti, S

Subjects
Saccharomyces cerevisiae Proteins, cells, genetic processes, Mitosis, Cell Cycle Proteins, BIO/18 - GENETICA, macromolecular substances, Saccharomyces cerevisiae, Spindle Apparatus, Polo-like kinase, environment and public health, Article, mitotic checkpoints, adaptation, RSC, Cdc14,yeast, chemistry.chemical_compound, Phosphoprotein Phosphatases, Chromatin structure remodeling (RSC) complex, Research Articles, Anaphase, biology, Cdc14, Cell Biology, Chromatin Assembly and Disassembly, Cell biology, Genes, cdc, Nocodazole, Spindle checkpoint, chemistry, Mitotic exit, biology.protein, Protein Tyrosine Phosphatases, Signal Transduction
Abstract

Rsc2 promotes Cdc14 release from the nucleolus to free cells from mitotic arrest., Upon prolonged activation of the spindle assembly checkpoint, cells escape from mitosis through a mechanism called adaptation or mitotic slippage, which is thought to underlie the resistance of cancer cells to antimitotic drugs. We show that, in budding yeast, this mechanism depends on known essential and nonessential regulators of mitotic exit, such as the Cdc14 early anaphase release (FEAR) pathway for the release of the Cdc14 phosphatase from the nucleolus in early anaphase. Moreover, the RSC (remodel the structure of chromatin) chromatin-remodeling complex bound to its accessory subunit Rsc2 is involved in this process as a novel component of the FEAR pathway. We show that Rsc2 interacts physically with the polo kinase Cdc5 and is required for timely phosphorylation of the Cdc14 inhibitor Net1, which is important to free Cdc14 in the active form. Our data suggest that fine-tuning regulators of mitotic exit have important functions during mitotic progression in cells treated with microtubule poisons and might be promising targets for cancer treatment.

Published
2010

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