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Titolo:
p120(ctn) acts as an inhibitory regulator of cadherin function in colon carcinoma cells
Autore:
Aono, S; Nakagawa, S; Reynolds, AB; Takeichi, M;
Indirizzi:
Kyoto Univ, Fac Sci, Dept Biophys, Sakyo Ku, Kyoto 6068502, Japan Kyoto Univ Kyoto Japan 6068502 t Biophys, Sakyo Ku, Kyoto 6068502, Japan Vanderbilt Univ, Sch Med, Dept Cell Biol, Nashville, TN 37232 USA Vanderbilt Univ Nashville TN USA 37232 Cell Biol, Nashville, TN 37232 USA
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 3, volume: 145, anno: 1999,
pagine: 551 - 562
SICI:
0021-9525(19990503)145:3<551:PAAAIR>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
TYROSINE KINASE SUBSTRATE; ARMADILLO FAMILY MEMBER; ALPHA-CATENIN; BETA-CATENIN; CYTOPLASMIC DOMAIN; ADHESION SYSTEM; DESMOSOMAL PLAQUE; EPITHELIAL-CELLS; N-CADHERIN; PROTEIN;
Keywords:
E-cadherin; catenin; colon carcinoma; Colo 205; p120(ctn);
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
67
Recensione:
Indirizzi per estratti:
Indirizzo: Takeichi, M Kyoto Univ, Fac Sci, Dept Biophys, Sakyo Ku, Kyoto 6068502, Japan Kyoto Univ Kyoto Japan 6068502 akyo Ku, Kyoto 6068502, Japan
Citazione:
S. Aono et al., "p120(ctn) acts as an inhibitory regulator of cadherin function in colon carcinoma cells", J CELL BIOL, 145(3), 1999, pp. 551-562

Abstract

p120(ctn) binds to the cytoplasmic domain of cadherins but its role is poorly understood. Cole 205 cells grow as dispersed cells despite their normalexpression of E-cadherin and catenins. However, in these cells we can induce typical E-cadherin-dependent aggregation by treatment with staurosporineor trypsin. These treatments concomitantly induce an electrophoretic mobility shift of p120(ctn) to a faster position. To investigate whether p120(ctn) plays a role in this cadherin reactivation process, we transfected Cole 205 cells with a series of p120(ctn) deletion constructs. Notably, expression of NH2-terminally deleted p120(ctn) induced aggregation. Similar effectswere observed when these constructs were introduced into HT-29 cells. Whena mutant N-cadherin lacking the p120(ctn)-binding site was introduced intoCole 205 cells, this molecule also induced cell aggregation, indicating that cadherins can function normally if they do not bind to p120(ctn). These findings suggest that in Cole 205 cells, a signaling mechanism exists to modify a biochemical state of p120(ctn) and the modified p120(ctn) blocks thecadherin system. The NH2 terminus-deleted p120(ctn) appears to compete with the endogenous p120(ctn) to abolish the adhesion-blocking action.

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Documento generato il 07/07/20 alle ore 12:27:56