First published online December 31, 2003
Journal of Cell Science 117, 304e (2004)
© The Company of Biologists Limited
APC adheres
The adenomatous polyposis coli protein (APC) is a tumour suppressor that binds to ß-catenin – the Wnt/Wingless signalling pathway component that moves from cadherin-based adherens junctions at the plasma membrane to the nucleus and stimulates expression of genes that control cell proliferation. APC prevents ß-catenin from relaying proliferative signals to the nucleus, and APC mutants that cannot bind to ß-catenin are associated with deregulated cell proliferation in colon cancer. But does APC have a role in cell adhesion, given that ß-catenin is also a component of adherens junctions? Maree Faux and co-workers have answered this question by stably introducing wild-type APC into colon cancer cells expressing mutated APC (see p. 427). They show this causes ß-catenin to return from the nucleus to the cell periphery, where it forms functional adherens junctions. Significantly, E-cadherin levels are increased in the transfected cells, and E-cadherin redistributes from the cytoplasm to the plasma membrane. Furthermore, this is associated with increased cell adhesion, changes in cell morphology and reduced proliferation. The authors' observations reveal for the first time that APC plays an important role in cell adhesion as a regulator of both ß-catenin and E-cadherin localization, which could be essential for tumour suppression.
Related articles in JCS:
- Restoration of full-length adenomatous polyposis coli (APC) protein in a colon cancer cell line enhances cell adhesion
- Maree C. Faux, Janine L. Ross, Clare Meeker, Terry Johns, Hong Ji, Richard J. Simpson, Meredith J. Layton, and Antony W. Burgess
JCS 2004 117: 427-439.
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