Calreticulin Affects β-Catenin-associated Pathways

Calreticulin, a Ca 2+ storage protein and chaperone in the endoplasmic reticulum, also modulates cell adhesiveness. Overexpression of calreticulin correlates with (i) increased cell adhesiveness, (ii) increased expression of N-cadherin and vinculin, and (iii) decreased protein phosphorylation on tyr...

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Bibliographic Details
Published in:The Journal of biological chemistry 2001-07, Vol.276 (29), p.27083
Main Authors: Marc P. Fadel, Malgorzata Szewczenko-Pawlikowski, Pierre Leclerc, Ewa Dziak, J. Matthew Symonds, Orest Blaschuk, Marek Michalak, Michal Opas
Format: Article
Language:English
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Summary:Calreticulin, a Ca 2+ storage protein and chaperone in the endoplasmic reticulum, also modulates cell adhesiveness. Overexpression of calreticulin correlates with (i) increased cell adhesiveness, (ii) increased expression of N-cadherin and vinculin, and (iii) decreased protein phosphorylation on tyrosine. Among proteins that are dephosphorylated in cells that overexpress calreticulin is β-catenin, a structural component of cadherin-dependent adhesion complexes, a member of the armadillo family of proteins and a part of the Wnt signaling pathway. We postulate that the changes in cell adhesiveness may be due to calreticulin-mediated effects on a signaling pathway from the endoplasmic reticulum, which impinges on the Wnt signaling pathway via the cadherin/catenin protein system and involves changes in the activity of protein-tyrosine kinases and/or phosphatases.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M101676200