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Titolo:
The amino- and carboxyl-terminal tails of beta-catenin reduce its affinityfor desmoglein 2
Autore:
Wahl, JK; Nieset, JE; Sacco-Bubulya, PA; Sadler, TM; Johnson, KR; Wheelock, MJ;
Indirizzi:
Univ Toledo, Dept Biol, Toledo, OH 43606 USA Univ Toledo Toledo OH USA 43606 v Toledo, Dept Biol, Toledo, OH 43606 USA
Titolo Testata:
JOURNAL OF CELL SCIENCE
fascicolo: 10, volume: 113, anno: 2000,
pagine: 1737 - 1745
SICI:
0021-9533(200005)113:10<1737:TAACTO>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
JUNCTIONAL PLAQUE PROTEIN; CELL-CELL ADHESION; EPITHELIAL-CELLS; ALPHA-CATENIN; DESMOSOMAL CADHERINS; FUNCTIONAL INTERACTION; PLAKOGLOBIN DOMAINS; CYTOPLASMIC DOMAIN; ACID-SEQUENCE; N-CADHERIN;
Keywords:
beta-catenin; desmoglein; plakoglobin; N-cadherin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Wheelock, MJ Univ Toledo, Dept Biol, Toledo, OH 43606 USA Univ Toledo Toledo OH USA 43606 t Biol, Toledo, OH 43606 USA
Citazione:
J.K. Wahl et al., "The amino- and carboxyl-terminal tails of beta-catenin reduce its affinityfor desmoglein 2", J CELL SCI, 113(10), 2000, pp. 1737-1745

Abstract

Beta-catenin and plakoglobin are members of the armadillo family of proteins and were first identified as components of intercellular adhering junctions. In the adherens junction beta-catenin and plakoglobin serve to link classical cadherins to the actin-based cytoskeleton. In the desmosome plakoglobin links the desmosomal cadherins, the desmogleins and the desmocollins, to the intermediate filament cytoskeleton, beta-catenin is not a component of the desmosome. Previously we have shown that the central armadillo repeat region of plakoglobin is the site for desmosomal cadherin binding. We hypothesized that the unique amino- and/or carboxyl-terminal ends of beta-catenin may regulate its exclusion from the desmosomal plaque. To test this hypothesis we used chimeras between beta-catenin and plakoglobin to identify domain(s) that modulate association with desmoglein 2. Chimeric constructs, each capable of associating with classical cadherins, were assayed for association with the desmosomal cadherin desmoglein 2, Addition of either the N- or C-terminal tail of beta-catenin to the armadillo repeats of plakoglobin did not interfere with desmoglein 2 association. However, when both beta-catenin amino terminus and carboxyl terminus were added to the plakoglobin armadillo repeats, association with desmoglein 2 was diminished. Removal ofthe first 26 amino acids from this construct restored association, We showevidence for direct protein-protein interactions between the amino- and carboxyl-terminal tails of beta-catenin and propose that a sequence in the first 26 amino acids of beta-catenin along with its carboxyl-terminal tail decrease its affinity for desmoglein and prevent its inclusion in the desmosome.

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Documento generato il 20/09/20 alle ore 08:00:38