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Beta-Catenin Interactions
Published by Anonymous on 2007/9/29 (2170 reads)
1: J Cell Sci. 2000 Sep;113 ( Pt 18):3127-39.

Plakoglobin and beta-catenin: protein interactions, regulation and biological roles.

Zhurinsky J, Shtutman M, Ben-Ze'ev A.

Department of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot, Israel.

Beta-catenin can play different roles in the cell, including one as a structural protein at cell-cell adherens junctions and another as a transcriptional activator mediating Wnt signal transduction. Plakoglobin (gamma)-catenin), a close homolog of beta-catenin, shares with beta-catenin common protein partners and can fulfill some of the same functions. The complexing of catenins with various protein partners is regulated by phosphorylation and by intramolecular interactions. The competition between different catenin partners for binding to catenins mediates the cross-talk between cadherin-based adhesion, catenin-dependent transcription and Wnt signaling. Although plakoglobin differs from beta-catenin in its functions and is unable to compensate for defects in Wnt signaling resulting from lack of beta-catenin, recent evidence suggests that plakoglobin plays a unique role in Wnt signaling that is different from that of beta-catenin. The functional difference between catenins is reflected in their differential involvement in embryonic development and cancer progression.

Publication Types:
Research Support, Non-U.S. Gov't

PMID: 10954412 [PubMed - indexed for MEDLINE]


2: Curr Opin Cell Biol. 1998 Oct;10(5):629-39.

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

Ben-Ze'ev A, Geiger B.

Department of Molecular Cell Biology, Weizmann Institute of Science, Rehovot, Israel. lgbenzev@weizmann.weizmann.ac.il

Plakoglobin and beta-catenin are homologous proteins functioning in cell adhesion and transactivation. Their activities are controlled by three types of interactions: those with cadherins in adherens junctions, linking them to the actin cytoskeleton; interactions in the nucleus, where they bind to transcription factors and stimulate gene expression; interactions of free cytoplasmic beta-catenin with axin and adenomatous polyposis coli (APC) protein which target it for degradation. Studies in the past year have demonstrated the complex interplay between these three types of interactions and the different behavior of beta-catenin and plakoglobin in their involvement in morphogenesis and tumorigenesis strongly suggesting that catenins play key roles in adhesion-mediated signaling.

Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

PMID: 9818174 [PubMed - indexed for MEDLINE]


3: J Pathol. 1997 Jun;182(2):128-37.

The interactions of APC, E-cadherin and beta-catenin in tumour development and progression.

Ilyas M, Tomlinson IP.

Cancer Genetics and Immunology Laboratory, Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, Oxon, U.K.

Much progress has been made in identifying genes mutated during the development of colorectal carcinoma. Mutation of the APC gene in particular appears to be fundamental for colorectal tumour initiation. In contrast, loss of expression of E-cadherin appears to be a late event, which may be important in the development of invasion. Recent clarification of the function of APC, however, has shown that it exists in equilibrium with beta-catenin and E-cadherin. This review discusses the function of these molecules, their interactions, and how APC mutations may alter the equilibrium with beta-catenin and E-cadherin. It is argued that these changes cause aberrant architectural development of tissue, which results in loss of growth control. It is this escape from growth control, rather than acquisition of cell-autonomous growth, which results in the initial development of adenomas. The role of the E-cadherin-catenin unit in colorectal tumour invasion is discussed and the evidence is reviewed for the involvement of APC and E-cadherin in tumours arising from non-intestinal epithelia.

Publication Types:

PMID: 9274521 [PubMed - indexed for MEDLINE]

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