Differential molecular interactions of β-catenin and plakoglobin in adhesion, signaling and cancer

Current Opinion in Cell Biology

Volumn 10, Issue 5, 1998, Pages 629-639

  Ben Ze'Ev, Avri ^a   Geiger, Benjamin ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BETA CATENIN; CADHERIN; CYTOPLASM PROTEIN; PLAKOGLOBIN; TRANSCRIPTION FACTOR;

ANIMAL CELL; CARCINOGENESIS; CELL ADHESION; COLON POLYPOSIS; CYTOSKELETON; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; MOLECULAR INTERACTION; MORPHOGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PROTEIN INTERACTION; REVIEW; SIGNAL TRANSDUCTION; TRANSACTIVATION;

ANIMALIA;

EID: 0031718204     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80039-2     Document Type: Article

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86. Rubinfeld B, Robbins P, El-Gamil M, Albert I, Porfiri E, Polakis P. Stabilization of β-catenin by genetic defects in melanoma cell lines. of outstanding interest Science. 275:1997;1790-1792 This is the first demonstration in human melanoma of increased β-catenin levels owing either to mutations in the adenomatous polyposis coli (APC) gene or to mutations in the amino-terminal serine residues of β-catenin that are phosphorylated by glycogen synthase kinase 3β and that are important for the regulation of β-catenin degradation. In addition, these cells were shown to contain constitutive β-catenin - lymphoid enhancer binding factor (LEF)-1 complexes, suggesting that these are involved in tumor progression in melanoma.
87. Peifer M. β-catenin as oncogene: the smoking gun. of outstanding interest of special interest Science. 275:1997;1752-1753 This is a very attractively written review on the important breakthrough presented in [84-86] suggesting that β-catenin can act as an oncogene.
88. Tsukamoto AS, Grosschedl R, Guzman RC, Parslow T, Varmus HE. Expression of the int-1 gene in transgenic mice is associated with mammary gland hyperplasia and adenocarcinomas in male and female mice. Cell. 55:1988;619-625.
89. Whitehead I, Kirk H, Kay R. Expression cloning of oncogenes by retroviral transfer of cDNA libraries. Mol Cell Biol. 15:1995;704-710.
90. Rubinfeld B, Albert I, Porfiri E, Munemitsu S, Polakis P. Loss of β-catenin regulation by the APC tumor suppressor protein correlates with loss of structure due to common somatic mutations of the gene. of special interest Cancer Res. 20:1997;4624-4630 This study demonstrates that the somatic mutations in adenomatous polyposis coli (APC) seen in human colon cancers that are clustered in a very narrow region of the gene are localized on the APC molecule in a domain that is responsible for regulating the binding and degradation of β-catenin, suggesting that this site is selected for during tumor progression.
91. Sparks AB, Morin PJ, Vogelstein B, Kinzler KW. Mutational analysis of the APC/β-catenin/Tcf pathway in colorectal cancer. of special interest Cancer Res. 58:1998;1130-1134 In this study, the authors searched for possible mutations in the genes for β-catenin, adenomatous polyposis coli (APC) and other components of the Wnt pathway in colon cancers, and found mutations in either β-catenin or APC, but not other known components of the pathway. These mutations were mutually exclusive (either in β-catenin or in APC) and thus equivalent, since both affect the stability of β-catenin. This further supports the role of changes in β-catenin stability in colon cancer.
92. Zurawel RH, Chippa SA, Allen C, Raffael C. Sporadic medulloblastomas contain oncogenic β-catenin mutations. of special interest Cancer Res. 58:1998;896-899 See annotation to [94].
93. Palacios J, Gamallo C. Mutations in the β-catenin gene (CTNNB1) in endometroid ovarian carcinomas. of special interest Cancer Res. 58:1998;1344-1347 See annotation to [94].
94. Takahashi M, Fukuda K, Sugimura T, Wakabayashi K. β-catenin is frequently mutated and demonstrates altered cellular location in azoxymethane-induced rat colon tumors. of outstanding interest of special interest Cancer Res. 58:1998;42-46 This study and the ones in [92,93] describe mutations in the amino terminus of the β-catenin gene that have been shown to be responsible for regulating the stability of β-catenin in other types of cancer, in addition to colon cancer [84,85,91] and melanoma [86], suggesting that such mutations may play a role in tumor progression in a larger variety of human cancers than was previously recognized.
95. Aberle H, Bierkamp C, Torchard D, Serova O, Wagener T, Natt E, Wirsching J, Heidkamper C, Montagna M, Lynch HT, Lenoir GM, et al. The human plakoglobin gene localizes on chromosome 17q21 and is subject to loss of heterozygosity in breast and ovarian cancer. Proc Natl Acad Sci USA. 92:1995;6384-6388.
96. Vleminckx KL, Vakaet J, Mareel M, Fiers W, Van Roy F. Genetic manipulation of E-cadherin expression by epithelial tumor cells reveals an invasion suppressor role. Cell. 66:1991;107-119.
97. Bullions LC, Notterman DA, Chung LS, Levine AJ. Expression of a wild type α-catenin protein in cells with a mutant α-catenin gene restores both growth regulation and tumor suppression activities. Mol Cell Biol. 17:1997;4501-4508.