Independent interactions of phosphorylated β-catenin with E-cadherin at cell-cell contacts and APC at cell protrusions.

ABSTRACT:

Background

The APC tumour suppressor functions in several cellular processes including the regulation of β-catenin in Wnt signalling and in cell adhesion and migration.

Findings

In this study, we establish that in epithelial cells N-terminally phosphorylated β-catenin specifically localises to several subcellular sites including cell-cell contacts and the ends of cell protrusions. N-terminally phosphorylated β-catenin associates with E-cadherin at adherens junctions and with APC in cell protrusions. We isolated APC-rich protrusions from stimulated cells and detected β-catenin, GSK3β and CK1α, but not axin. The APC/phospho-β-catenin complex in cell protrusions appears to be distinct from the APC/axin/β-catenin destruction complex. GSK3β phosphorylates the APC-associated popul

SUBMITTER: Faux MC 

PROVIDER: S-EPMC2994709 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature