Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Pin 1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC
Autore:
Ryo, A; Nakamura, M; Wulf, G; Liou, YC; Lu, KP;
Indirizzi:
Beth Israel Deaconess Med Ctr, Dept Med, Div Hematol Oncol, Canc Biol Program, Boston, MA 02215 USA Beth Israel Deaconess Med Ctr Boston MA USA 02215 m, Boston, MA 02215 USA Harvard Univ, Sch Med, Boston, MA 02215 USA Harvard Univ Boston MA USA 02215 vard Univ, Sch Med, Boston, MA 02215 USA
Titolo Testata:
NATURE CELL BIOLOGY
fascicolo: 9, volume: 3, anno: 2001,
pagine: 793 - 801
SICI:
1465-7392(200109)3:9<793:P1RTAS>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
TUMOR-SUPPRESSOR PROTEIN; DEPENDENT PROLINE ISOMERIZATION; HUMAN BREAST-CANCER; CELL-CYCLE; PROLYL ISOMERIZATION; XENOPUS EMBRYOS; COLON-CARCINOMA; COMPLEX; IDENTIFICATION; ASSOCIATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Lu, KP Beth Israel Deaconess Med Ctr, Dept Med, Div Hematol Oncol, Canc Biol Program, 330 Brookline Ave, Boston, MA 02215 USA Beth Israel Deaconess Med Ctr 330 Brookline Ave Boston MA USA 02215
Citazione:
A. Ryo et al., "Pin 1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC", NAT CELL BI, 3(9), 2001, pp. 793-801

Abstract

Phosphorylation on a serine or threonine residue preceding proline (Ser/Thr-Pro) is a key regulatory mechanism, and the conformation of certain phosphorylated Ser/Thr-Pro bonds is regulated specifically by the prolyl isomerase Pin1. Whereas the inhibition of Pin1 induces apoptosis, Pin1 is strikingly overexpressed in a subset of human tumours. Here we show that Pin1 regulates beta -catenin turnover and subcellular localization by interfering with its interaction with adenomatous polyposis coli protein (APC). A differential-display screen reveals that Pin1 increases the transcription of several beta -catenin target genes, including those encoding cyclin D1 and c-Myc. Manipulation of Pin1 levels affects the stability of beta -catenin in vitro. Furthermore, beta -catenin levels are decreased in Pin1-deficient mice but are increased and correlated with Pin1 overexpression in human breast cancer. Pin1 directly binds a phosphorylated Ser-Pro motif next to the APC-binding site in beta -catenin, inhibits its interaction with APC and increases its translocation into the nucleus. Thus, Pin1 is a novel regulator of beta -catenin signalling and its overexpression might contribute to the upregulation of beta -catenin in tumours such as breast cancer, in which APC or beta -catenin mutations are not common.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 08:18:49