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Titolo:
Selective uncoupling of p120(ctn) from E-cadherin disrupts strong adhesion
Autore:
Thoreson, MA; Anastasiadis, PZ; Daniel, JM; Ireton, RC; Wheelock, MJ; Johnson, KR; Hummingbird, DK; Reynolds, AB;
Indirizzi:
Vanderbilt Univ, Dept Cell Biol, Sch Med, Nashville, TN 37232 USA Vanderbilt Univ Nashville TN USA 37232 , Sch Med, Nashville, TN 37232 USA 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 BIOLOGY
fascicolo: 1, volume: 148, anno: 2000,
pagine: 189 - 201
SICI:
0021-9525(20000110)148:1<189:SUOPFE>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-CELL-ADHESION; TYROSINE KINASE SUBSTRATE; CATENIN COMPLEX-FORMATION; TUMOR-SUPPRESSOR PROTEIN; MOLECULES ALPHA-CATENINS; HUMAN COLORECTAL-CANCER; ROUS-SARCOMA VIRUS; BETA-CATENIN; CYTOPLASMIC DOMAIN; TRANSFORMING PROTEIN;
Keywords:
metastasis; catenin; compaction; clustering; adherens junction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
77
Recensione:
Indirizzi per estratti:
Indirizzo: Reynolds, AB Vanderbilt Univ, Dept Cell Biol, Sch Med, MCN C-2310, Nashville, TN 37232 USA Vanderbilt Univ MCN C-2310 Nashville TN USA 37232 N 37232 USA
Citazione:
M.A. Thoreson et al., "Selective uncoupling of p120(ctn) from E-cadherin disrupts strong adhesion", J CELL BIOL, 148(1), 2000, pp. 189-201

Abstract

p120(ctn) is a catenin whose direct binding to the juxtamembrane domain ofclassical cadherins suggests a role in regulating cell-cell adhesion. The juxtamembrane domain has been implicated in a variety of roles including cadherin clustering, cell motility, and neuronal outgrowth, raising the possibility that p120 mediates these activities. We have generated minimal mutations in this region that uncouple the E-cadherin-p120 interaction, but do not affect interactions with other catenins, By stable transfection into E-cadherin-deficient cell lines, we show that cadherins are both necessary andsufficient for recruitment of p120 to junctions. Detergent-free subcellular fractionation studies indicated that, in contrast to previous reports, the stoichiometry of the interaction is extremely high. Unlike alpha- and beta-catenins, p120 was metabolically stable in cadherin-deficient cells, and was present at high levels in the cytoplasm. Analysis of cells expressing E-cadherin mutant constructs indicated that p120 is required for the E-cadherin-mediated transition from weak to strong adhesion. In aggregation assays, cells expressing p120-uncoupled E-cadherin formed only weak cell aggregates, which immediately dispersed into single cells upon pipetting. As an apparent consequence, the actin cytoskeleton failed to insert properly into peripheral E-cadherin plaques, resulting in the inability to form a continuous circumferential ring around cell colonies. Our data suggest that p120 directly or indirectly regulates lates the E-cadherin-mediated transition to tight cell-cell adhesion, possibly blocking subsequent events necessary for reorganization of the actin cytoskeleton and compaction.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 05:34:06