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Titolo:
Regulation of beta-catenin structure and activity by tyrosine phosphorylation
Autore:
Piedra, J; Martinez, D; Castano, J; Miravet, S; Dunach, M; de Herreros, AG;
Indirizzi:
Univ Pompeu Fabra, Inst Municipal Invest Med, Unit Biol Cellular & Mol, Barcelona 08003, Spain Univ Pompeu Fabra Barcelona Spain 08003 ar & Mol, Barcelona 08003, Spain Univ Autonoma Barcelona, Fac Med, Dept Bioquim & Biol Mol, Unit Biofis, Bellaterra 08193, Spain Univ Autonoma Barcelona Bellaterra Spain 08193 , Bellaterra 08193, Spain
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 23, volume: 276, anno: 2001,
pagine: 20436 - 20443
SICI:
0021-9258(20010608)276:23<20436:ROBSAA>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-ADHESION; E-CADHERIN; TRANSCRIPTIONAL COACTIVATOR; MEDIATED TRANSCRIPTION; BINDING PROTEIN; COLON-CARCINOMA; IN-VITRO; COMPLEX; ARMADILLO; APC;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Dunach, M Univ Pompeu Fabra, Inst Municipal Invest Med, Unit Biol Cellular& Mol, C-Dr Aiguador 80, Barcelona 08003, Spain Univ Pompeu Fabra C-Dr Aiguador 80 Barcelona Spain 08003 Spain
Citazione:
J. Piedra et al., "Regulation of beta-catenin structure and activity by tyrosine phosphorylation", J BIOL CHEM, 276(23), 2001, pp. 20436-20443

Abstract

beta -Catenin plays a dual role as a key effector in the regulation of adherens junctions and as a transcriptional coactivator. Phosphorylation of Tyr-654, a residue placed in the last armadillo repeat of beta -catenin, decreases its binding to E-cadherin. We show here that phosphorylation of Tyr-654 also stimulates the association of beta -catenin to the basal transcription factor TATA-binding protein. The structural bases of these different affinities were investigated. Our results indicate that the beta -catenin C-terminal tail interacts with the armadillo repeat domain, hindering the association of the armadillo region to the TATA-binding protein or to E-cadherin. Phosphorylation of beta -catenin Tyr-654 decreases armadillo-C-terminal tail association, uncovering the last armadillo repeats. in a C-terminal-depleted beta -catenin, the presence of a negative charge at Tyr-654 does notaffect the interaction of the TATA-binding protein to the armadillo domain. However, in the case of E-cadherin, the establishment of ion pairs dominates its association with beta -catenin, and its binding is greatly dependent on the absence of a negative charge at Tyr-654. Thus, phosphorylation of Tyr-654 blocks the E-cadherin-beta -catenin interaction, even though the steric hindrance of the C-tail is no longer present. These results explain how phosphorylation of beta -catenin in Tyr-654 modifies the tertiary structure of this protein and the interaction with its different partners.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 06:31:09