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Titolo:
DESMOSOMAL CADHERIN BINDING DOMAINS OF PLAKOGLOBIN
Autore:
WITCHER LL; COLLINS R; PUTTAGUNTA S; MECHANIC SE; MUNSON M; GUMBINER B; COWIN P;
Indirizzi:
NYU,MED CTR,DEPT CELL BIOL,550 1ST AVE NEW YORK NY 10016 NYU,MED CTR,DEPT CELL BIOL NEW YORK NY 10016 NYU,MED CTR,RONALD O PERELMAN DEPT DERMATOL NEW YORK NY 10016 NYU,MED CTR,KAPLAN CANC CTR NEW YORK NY 10016 MEM SLOAN KETTERING CANC CTR NEW YORK NY 10021
Titolo Testata:
The Journal of biological chemistry
fascicolo: 18, volume: 271, anno: 1996,
pagine: 10904 - 10909
SICI:
0021-9258(1996)271:18<10904:DCBDOP>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
SEGMENT POLARITY GENE; CELL-ADHESION MOLECULE; JUNCTIONAL PLAQUE PROTEIN; BETA-CATENIN; DROSOPHILA HOMOLOG; EPITHELIAL-CELLS; ARMADILLO; ASSOCIATION; UVOMORULIN; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
51
Recensione:
Indirizzi per estratti:
Citazione:
L.L. Witcher et al., "DESMOSOMAL CADHERIN BINDING DOMAINS OF PLAKOGLOBIN", The Journal of biological chemistry, 271(18), 1996, pp. 10904-10909

Abstract

Plakoglobin is a major component of both desmosomes and adherens junctions. At these sites it binds to the cytoplasmic domains of cadherin cell-cell adhesion proteins and regulates their adhesive and cytoskeletal binding functions. Plakoglobin also forms distinct cytosolic protein complexes that function in pathways of tumor suppression and cell fate determination. Recent studies in Xenopus suggest that cadherins inhibit the signaling functions of plakoglobin presumably by sequestering this protein at the membrane and depleting its cytosolic pool. To understand the reciprocal regulation between desmosomal cadherins (desmoglein and desmocollin) and plakoglobin, we have sought to identify thebinding domains involved in the formation of these protein complexes. Plakoglobin comprises 13 central repeats flanked by amino-terminal and carboxyl-terminal domains. Our results show that repeats 1-4 are involved in binding desmoglein-1. In contrast, the interaction of plakoglobin with desmocollin-1a is sensitive to deletion of either end of thecentral repeat domain. The binding sites for two adherens junction components, alpha-catenin and classical cadherins, overlap these sites. Competition among these proteins for binding sites on plakoglobin may therefore account for the distinct composition of adherens junctions and desmosomes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 02:00:07