Direzione e uffici C.I.B.

Direzione CIB:
Prof. Claudio Schneider
Email: claudio.schneider@Lncib.it

Segreteria CIB:
Prof. Roberto Gambari
Email: roberto.gambari@unife.it

SEGRETERIA ORGANIZZATIVA:
Elisabetta Lambertini
Tel: 0532/974451
Fax: 0532/974484
E-mail: lmblbt@unife.it

AMMINISTRAZIONE:
Vanessa Florit
Area di Ricerca
Padriciano, 99 - 34012 Trieste
Tel: 040/398979
Fax: 040/398990
E-mail: cib@lncib.it

Posta certificata C.I.B.:
cib@poste-certificate.it

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Del Sal Giannino Stampa
RESPONSABILE DELLA U. O.

Cognome e Nome
Del Sal Giannino
Qualifica
PO
Facoltà
BBCM/LNCIB
Dipartimento
Settore Scientifico Disciplinare
BIO13
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PERSONALE STRUTTURATO

Cognome e Nome
Licio Collavin
Qualifica
RC-(SSD-BIO13)
Dipartimento
BBCM
Ente di appartenenza
LNCIB
Cognome e Nome
Qualifica
Dipartimento
Ente di appartenenza
Cognome e Nome
Qualifica
Dipartimento
Ente di appartenenza
Cognome e Nome
Qualifica
Dipartimento
Ente di appartenenza

PERSONALE NON STRUTTURATO

Cognome e Nome
Alessandra Rustighi
Qualifica
Senior post doc Borsista
Dipartimento
BBCM
Ente di appartenenza
LNCIB
Cognome e Nome
Andrea Bisso
Qualifica
studente PhD
Dipartimento
BBCM
Ente di appartenenza
LNCIB
Cognome e Nome
Anrea Lunardi
Qualifica
Senior post doc Borsista
Dipartimento
BBCM
Ente di appartenenza
LNCIB
Cognome e Nome
Elisa Guida
Qualifica
studente PhD
Dipartimento
BBCM
Ente di appartenenza
LNCIB
Cognome e Nome
Fiamma Mantovani
Qualifica Senior Post Doc /Assegnista
Dipartimento
BBCM
Ente di appartenenza
LNCIB
Cognome e Nome
Francesca Tocco
Qualifica studente PhD
Dipartimento
BBCM
Ente di appartenenza
LNCIB
Cognome e Nome
Fulvio Chiacchera
Qualifica studente PhD
Dipartimento
BBCM
Ente di appartenenza
LNCIB
Cognome e Nome
Javier Girardini
Qualifica
Post doc Borsista
Dipartimento
BBCM
Ente di appartenenza
LNCIB
Cognome e Nome
Luca Tiberi
Qualifica
studente PhD
Dipartimento
BBCM
Ente di appartenenza
LNCIB
Cognome e Nome
Tizia Macorig
Qualifica
studente PhD
Dipartimento
BBCM
Ente di appartenenza
LNCIB
Cognome e Nome
Qualifica
Dipartimento
Ente di appartenenza

LINEE DI RICERCA

The tumor suppressor gene p53 is frequently mutated in a wide variety of human cancers. p53 induces the expression of several genes whose products regulate cell cycle, DNA repair, metabolic processes and susceptibility to apoptosis. The large number of signalling pathways that regulate p53 activation, combined with the composite pattern of covalent modifications and protein interactions required to coordinate p53-dependent response, indicate that p53 is an highly connected and critical “node” in the molecular network governing the life of a cell. Recently two p53 homologous genes, p63 and p73, have been identified in mammalian cells. These genes give rise to the expression of proteins that are similar to p53 in structure and function and induce some p53-responsive genes thus contributing to a more efficient physiological response upon stress stimuli with important implications in cancer treatment. Notably some tumor-derived mutant p53 bind and inactivate both p73 and p63, thus suggesting a possible mechanism for the observed “gain of function” phenotype displayed by some p53 mutants. Our Unit is focused on the molecular mechanisms governing the activation of p53 an p73 /p63 under normal and stressed conditions.

The research is divided in several lines:

-Understanding the role of postraslational modifications and protein interactions in regulating p53 and p73 transcriptional and pro-apoptotic activity.
-Understanding the“gain of function” of mutant p53.
-Screening of libraries of small peptide aptamers able to bind to mutantp53 and inhibit its functions. This approach is also useful for the identification of inhibitors of other proteins with relevant functions in tumor growth.
-Defining the complete p53 interactome in Drosophyla by small pool screening.
-Use of the Xenopus leavis to study functional interconections among p53 pathway and other signalling pathways in embrionic development and cancer progression.

TECNOLOGIE IN POSSESSO DELL'U. O.

  • Yeast two hybrid
  • microinjection of Xenopus leavis embryos and phenotypical analysis
  • FACS

STRUMENTAZIONE

Denominazione
Struttura ove la strumentazione è allocata
Responsabile della strumentazione

PUBBLICAZIONI

1. Berger,.M., Stahl N, Del Sal G., and Haupt Y. (2005) Mutations in proline 82 of p53 impairs its activation by Pin1 and Chk2 in response to DNA damage Mol Cell Biol 25:5380-8.
2. Gostissa, M. Morelli M. , Mantovani F., Guida E., Piazza, S., Collavin L., Brancolini C., Schneider C. and Del Sal G. (2004 )The transcriptional repressor hDaxx potentiates p53-dependent apoptosis. J.Biol. Chem 79: 48013-23.
3. Mantovani, F. Piazza S. Gostissa M. Strano S. Zacchi P., Blandino G and Del Sal G (2004).Pin1 regulates the stability and activity of p73 under normal and stress conditions. Mol Cell 4:625-36. IF. 16,835
4. Collavin L, Gostissa M, Avolio F, Secco P, Ronchi A, Santoro C, Del Sal G.Modification of the erythroid transcription factor GATA-1 by SUMO-1. (2004) Proc Natl Acad Sci U S A. (24):8870-5.
5. Collavin L, Kirschner MThe secreted Frizzled-related protein Sizzled functions as a negative feedback regulator of extreme ventral mesoderm. Development. 2003 130:805-16.
6. Gostissa M.,. Hoffman T, Will H and Del Sal G. (2003). Regulation of p53 functions:let’s meet at the Nucler Bodies. Current Opinion in Cell Biol. 2003 15:351-7.
7. Zacchi P. Gostissa M, Uchida T, Salvagno C, Avolio F, Volinia S, Ronai Z, Blandino G, Schneider C and Del Sal G.( 2002) The Prolyl-Isomerase Pin1 unveils a new mechanism to control p53 functions following genotoxic insults. Nature 419:853-7
8. G. D’Orazi, B. Cecchinelli, T. Brunot, I. Manni, Y. Higashimoto, S.Saito§, M. Gostissa, Sabrina Coen, A. Marchetti, G. Del Sal, Giulia Piaggio, M. Fanciulli, E. Appella and S. Soddu. (2002) Phosphorylation of p53 at Ser46 by the homeodomain-interacting protein kinase 2 mediates apoptosis. Nature Cell Biol. 1; 11-19.
9. Fogal V., Gostissa M.,Sandy P.,Zacchi P.,Jensen K., Sternsdorf T.,Pandolfi Will H.,Schneider C. and Del Sal. G. (2000). Regulation of p53 in Nuclear Bodies by a specific PML isoform. EMBO J 19:6185-6195.
10. Sandy,P., Gostissa, M., Fogal, V. DeCecco, L., Szalay, K., Roney, R. Schneider, C. and Del Sal G. (2000). p53 is involved in the p120E4F-mediated growth arrest. Oncogene 19: 188-199.

DOTTORATI DI RICERCA

Componente U.O. Dottorato di Ricerca Coordinatore Sede
Giannino del Sal
Medicina Molecolare
Giannino del sal

Giannino del Sal
Scienze biomolecolari
Franco Vittur

Licio Collavin
Medicina Molecolare
Giannino del Sal

CONGRESSI C.I.B.

Congressi Partecipazione
CNB4

CNB5

CNB6

CNB7

CNB8

CNB9
CNB10