The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
The APC Protein and E-cadherin Form Similar but Independent Complexes with α-Catenin, β-Catenin, and Plakoglobin
Open accessAbstract
The tumor suppressor APC protein associates with the cadherin-binding proteins alpha- and beta-catenin. To examine the relationship between cadherin, catenins, and APC, we have tested combinatorial protein-protein interactions in vivo, using a yeast two-hybrid system, and in vitro, using purified proteins. beta-Catenin directly binds to APC at high and low affinity sites. alpha-Catenin cannot directly bind APC but associates with it by binding to beta-catenin. Plakoglobin, also known as gamma-catenin, directly binds to both APC and alpha-catenin and also to the APC-beta-catenin complex, but not directly to beta-catenin. beta-Catenin binds to multiple independent regions of APC, some of which include a previously identified consensus motif and others which contain the centrally located 20 amino acid repeat sequences. The APC binding site on beta-catenin may be discontinuous since neither the carboxyl- nor amino-terminal halves of beta-catenin will independently associate with APC, although the amino-terminal half independently binds alpha-catenin. The catenins bind to APC and E-cadherin in a similar fashion, but APC and E-cadherin do not associate with each other either in the presence or absence of catenins. Thus, APC forms distinct heteromeric complexes containing combinations of alpha-catenin, beta-catenin, and plakoglobin which are independent from the cadherin-catenin complexes.
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Cites
Identification and characterization of the familial adenomatous polyposis coli gene
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Identification of FAP Locus Genes from Chromosome 5q21
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APC mutations occur early during colorectal tumorigenesis
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Self-citationAssociation of the APC Tumor Suppressor Protein with Catenins
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Cell binding function of E-cadherin is regulated by the cytoplasmic domain.
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Identification of deletion mutations and three new genes at the familial polyposis locus
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Cited by
Constitutive Transcriptional Activation by a β-Catenin-Tcf Complex in APC −/− Colon Carcinoma
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Caught up in a Wnt storm: Wnt signaling in cancer
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Ikeda, S. (1998) · The EMBO Journal · doi:10.1093/emboj/17.5.1371 · Cited by 1,246
The -Catenin Destruction Complex
Stamos, J. L., & Weis, W. I. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a007898 · Cited by 1,062
β-catenin: a key mediator of Wnt signaling
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Metadata
- Authors
- Rubinfeld, B., Souza, B., Albert, I., Munemitsu, S., & Polakis, P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-03
- Volume
- 270
- Issue
- 10
- Pages
- 5549-5555
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2071377606
- Cited by
- 310
- References
- 39
- FWCI
- 13.74
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: The APC Protein and E-cadherin Form Similar but Independent Complexes with α-Catenin, β-Catenin, and Plakoglobin. https://app.cochat.ai/papers/10.1074/jbc.270.10.5549
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- Rubinfeld, B., Souza, B., Albert, I., Munemitsu, S., & Polakis, P. (1995). The APC Protein and E-cadherin Form Similar but Independent Complexes with α-Catenin, β-Catenin, and Plakoglobin. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.270.10.5549
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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