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Your search keyword '"Onofri, Franco"' showing total 14 results
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14 results on '"Onofri, Franco"'

1. PRRT2 modulates presynaptic Ca2+ influx by interacting with P/Q-type channels

Author

Ferrante, Daniele, primary, Sterlini, Bruno, additional, Prestigio, Cosimo, additional, Marte, Antonella, additional, Corradi, Anna, additional, Onofri, Franco, additional, Tortarolo, Giorgio, additional, Vicidomini, Giuseppe, additional, Petretto, Andrea, additional, Muià, Jessica, additional, Thalhammer, Agnes, additional, Valente, Pierluigi, additional, Cingolani, Lorenzo A., additional, Benfenati, Fabio, additional, and Baldelli, Pietro, additional

Published
2021
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2. Synapsin III Controls Early Phases of Dopaminergic Neurons Development in Fishes and Mammals by Acting Upstream of BDNF and Cdk5 Signaling

Author

Faustini, Gaia, primary, Longhena, Francesca, additional, Muscò, Alessia, additional, Bono, Federica, additional, Parrella, Edoardo, additional, La Via, Luca, additional, Barbon, Alessandro, additional, Pizzi, Marina, additional, Onofri, Franco, additional, Benfenati, Fabio, additional, Missale, Cristina, additional, Memo, Maurizio, additional, Zizioli, Daniela, additional, Bellucci, Arianna, additional, and Administrator, Sneak Peek, additional

Published
2021
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3. PRRT2 Modulates Presynaptic Ca 2+ Influx by Interacting with P/Q-Type Channels

Author

Ferrante, Daniele, primary, Sterlini, Bruno, additional, Prestigio, Cosimo, additional, Marte, Antonella, additional, Corradi, Anna, additional, Onofri, Franco, additional, Petretto, Andrea, additional, Mujà, Jessica, additional, Thalhammer, Agnes, additional, Valente, Pierluigi, additional, Cingolani, Lorenzo, additional, Benfenati, Fabio, additional, and Baldelli, Pietro, additional

Published
2020
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6. PRRT2 Is a Key Component of the Ca 2+ -Dependent Neurotransmitter Release Machinery

Author

Valente, Pierluigi, primary, Castroflorio, Enrico, additional, Rossi, Pia, additional, Fadda, Manuela, additional, Sterlini, Bruno, additional, Cervigni, Romina Ines, additional, Prestigio, Cosimo, additional, Giovedì, Silvia, additional, Onofri, Franco, additional, Mura, Elisa, additional, Guarnieri, Fabrizia C., additional, Marte, Antonella, additional, Orlando, Marta, additional, Zara, Federico, additional, Fassio, Anna, additional, Valtorta, Flavia, additional, Baldelli, Pietro, additional, Corradi, Anna, additional, and Benfenati, Fabio, additional

Published
2016
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14. Specificity of the Binding of Synapsin I to Src Homology 3 Domains

Author

Pietro De Camilli, Silvia Giovedì, Flavia Valtorta, Paul Greengard, Hung-Teh Kao, Lucilla Bongiorno Borbone, Franco Onofri, Fabio Benfenati, Onofri, Franco, Giovedã¬, Silvia, Kao, Hung Teh, Valtorta, Flavia, Borbone, Lucilla Bongiorno, De Camilli, Pietro, Greengard, Paul, and Benfenati, Fabio

Subjects
Synapsin I, animal structures, Protein subunit, src Homology Domain, Rabbit, macromolecular substances, Biochemistry, Substrate Specificity, src Homology Domains, Adapter molecule crk, Animals, Molecular Biology, Actin, biology, Animal, Cell Biology, Synapsin, Synapsins, Cell biology, nervous system, biology.protein, Cattle, Rabbits, GRB2, Signal transduction, Protein Binding, Signal Transduction, Proto-oncogene tyrosine-protein kinase Src
Abstract

Synapsins are synaptic vesicle-associated phosphoproteins involved in synapse formation and regulation of neurotransmitter release. Recently, synapsin I has been found to bind the Src homology 3 (SH3) domains of Grb2 and c-Src. In this work we have analyzed the interactions between synapsins and an array of SH3 domains belonging to proteins involved in signal transduction, cytoskeleton assembly, or endocytosis. The binding of synapsin I was specific for a subset of SH3 domains. The highest binding was observed with SH3 domains of c-Src, phospholipase C-gamma, p85 subunit of phosphatidylinositol 3-kinase, full-length and NH(2)-terminal Grb2, whereas binding was moderate with the SH3 domains of amphiphysins I/II, Crk, alpha-spectrin, and NADPH oxidase factor p47(phox) and negligible with the SH3 domains of p21(ras) GTPase-activating protein and COOH-terminal Grb2. Distinct sites in the proline-rich COOH-terminal region of synapsin I were found to be involved in binding to the various SH3 domains. Synapsin II also interacted with SH3 domains with a partly distinct binding pattern. Phosphorylation of synapsin I in the COOH-terminal region by Ca(2+)/calmodulin-dependent protein kinase II or mitogen-activated protein kinase modulated the binding to the SH3 domains of amphiphysins I/II, Crk, and alpha-spectrin without affecting the high affinity interactions. The SH3-mediated interaction of synapsin I with amphiphysins affected the ability of synapsin I to interact with actin and synaptic vesicles, and pools of synapsin I and amphiphysin I were shown to associate in isolated nerve terminals. The ability to bind multiple SH3 domains further implicates the synapsins in signal transduction and protein-protein interactions at the nerve terminal level.

Published
2000

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