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Updated: Jun 23, 2026

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
Published on: October 17, 2014
Protein 4.1R links E-cadherin/beta-catenin complex to the cytoskeleton through its direct interaction with
Shaomin Yang1, Xinhua Guo, Gargi Debnath
1Red Cell Physiology Laboratory, New York Blood Center, 310 East 67th St., New York, NY 10065, USA.
Abstract:
Protein 4.1R (4.1R) is the prototypical member of the protein 4.1 superfamily comprising of the protein 4.1 family (4.1R, 4.1B, 4.1G and 4.1N) and ERM family (ezrin, radixin and meosin). These proteins in general serve as adaptors between the membrane and the cytoskeleton. Here we show that 4.1R expressed in the gastric epithelial cells associates with adherens junction protein beta-catenin. Biochemical examination of 4.1R-deficient stomach epithelia revealed a selective reduction of beta-catenin which is accompanied by a weaker linkage of E-cadherin to the cytoskeleton. In addition, organization of actin cytoskeleton was altered in 4.1R-deficient cells. Moreover, histological examination revealed that cell-cell contacts are impaired and gastric glands are disorganized in 4.1R null stomach epithelia. These results demonstrate an important and previously unidentified role of 4.1R in linking the cadherin/catenin complex to the cytoskeleton through its direct interaction with beta-catenin and in regulating the integrity of adherens junction.
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