The role of p120-ctn in regulating E-cadherin-mediated adhesion

Marita Kathleen Goodwin (2005). The role of p120-ctn in regulating E-cadherin-mediated adhesion PhD Thesis, School of Biomedical Sciences, The University of Queensland.

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Author Marita Kathleen Goodwin
Thesis Title The role of p120-ctn in regulating E-cadherin-mediated adhesion
School, Centre or Institute School of Biomedical Sciences
Institution The University of Queensland
Publication date 2005
Thesis type PhD Thesis
Supervisor Prof Alpha Yap
Prof Jennifer Stow
Total pages 213
Collection year 2005
Language eng
Subjects L
270105 Cellular Interactions (incl. Adhesion, Matrix, Cell Wall)
780105 Biological sciences
Formatted abstract

Classical cadherin adhesion molecules belong to a superfamily of cell surface glycoproteins, and are major participants in cell-cell adhesion. E-cadherin, the classical cadherin predominantly expressed in epithelial tissue, is a calcium-dependent, homophilic binding, single pass transmembrane protein that functions in cooperation with the actin cytoskeleton. It is increasingly apparent that E-cadherin operates as an adhesion-activated signalling receptor within the context of a dynamic macromolecular signalling complex. In particular, E-cadherin homophilic ligation can generate intracellular signals that potentially recruit, and activate, membrane or cytosolic proteins at adhesive contacts. The family of small RhoGTPases are one such group of proteins that become activated in direct response to E-cadherin ligation, and appear, in turn, to affect E-cadherin activity. In addition, as major regulators of the actin cytoskeleton, the RhoGTPases are prime candidates to influence E-cadherin and actin co-operativity. However, the molecular basis of an E-cadherin-RhoGTPase signalling pathway has not been elucidated, nor its precise contribution to E-cadherin function clearly understood. This dissertation has examined the contribution of pl20- ctn, a key component of the core cadherin/catenin complex that binds directly to the cadherin-JMD, to E-cadherin function. Using a minimal E-cadherin mutant that uncoupled pl20-ctn binding to the cadherin-JMD, in addition to E-cadherin specific signalling assays, this study reports that pl20-ctn is necessary for E-cadherin signalling to the RhoGTPase, Rac1. Perturbed E-cadherin-Rac signalling was accompanied by profound defects in the capacity for cells to establish cadherin-based contact and in cadherin-mediated adhesion. Therefore, this study provides evidence that pl20-ctn plays a central role in the E-cadherin-Rac signalling pathway. 

Keyword Cell receptors
Additional Notes Page 6 missing in the original thesis.

Document type: Thesis
Collection: UQ Theses (RHD) - UQ staff and students only
Citation counts: Google Scholar Search Google Scholar
Created: Fri, 24 Aug 2007, 18:45:22 EST