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Titolo:
A comparative evaluation of beta-catenin and plakoglobin signaling activity
Autore:
Williams, BO; Barish, GD; Klymkowsky, MW; Varmus, HE;
Indirizzi:
NCI, Div Basic Sci, NIH, Bethesda, MD 20892 USA NCI Bethesda MD USA 20892NCI, Div Basic Sci, NIH, Bethesda, MD 20892 USA Univ Colorado, Boulder, CO 80309 USA Univ Colorado Boulder CO USA 80309Univ Colorado, Boulder, CO 80309 USA
Titolo Testata:
ONCOGENE
fascicolo: 50, volume: 19, anno: 2000,
pagine: 5720 - 5728
SICI:
0950-9232(20001123)19:50<5720:ACEOBA>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
F-BOX PROTEIN; GLYCOGEN-SYNTHASE KINASE-3; TRANSCRIPTION FACTOR LEF-1; TUMOR-SUPPRESSOR PROTEIN; XENOPUS EMBRYOS; AXIS FORMATION; HEPATOCELLULAR CARCINOMAS; FUNCTIONAL INTERACTION; NUCLEAR-LOCALIZATION; NEGATIVE REGULATOR;
Keywords:
beta-catenin; plakoglobin; Wnt; LEF/TCF;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
87
Recensione:
Indirizzi per estratti:
Indirizzo: Williams, BO Van Andel Res Inst, 333 Bostwick NE, Grand Rapids, MI 49503 USA Van Andel Res Inst 333 Bostwick NE Grand Rapids MI USA 49503
Citazione:
B.O. Williams et al., "A comparative evaluation of beta-catenin and plakoglobin signaling activity", ONCOGENE, 19(50), 2000, pp. 5720-5728

Abstract

Vertebrates have two Armadillo-like proteins, beta -catenin and plakoglobin. Mutant forms of beta -catenin with oncogenic activity are found in many human tumors, but plakoglobin mutations are not commonly found, In fact, plakoglobin has been proposed to suppress tumorigenesis, To assess differences between beta -catenin and plakoglobin, we compared several of their biochemical properties, After transient transfection of 293T cells with an expression vector encoding either of the two proteins, soluble wild type beta -catenin does not significantly accumulate, whereas soluble wild type plakoglobin is readily detected. As anticipated, beta -catenin is stabilized by the oncogenic mutation S37A; however, the analogous mutation in plakoglobin (S28A) does not alter its half-life. S37A-beta -catenin activates a TCF/LEF-dependent reporter 20-fold more potently than wild type beta -catenin, and similar to5-fold more potently than wild type or S28A plakoglobin. These differences may be attributable to an enhanced affinity of S37A beta -cateninfor LEF1 and TCF4, as observed here by immunoprecipitation assays. We showthat the carboxyl-terminal domain is largely responsible for the difference in signaling and that the Armadillo repeats account for the remainder of the difference, The relatively weak signaling by plakoglobin and the failure of the S28A mutation to enhance its stability, may explain why plakoglobin mutations are infrequent in malignancies.

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Documento generato il 25/11/20 alle ore 10:13:24