Publications
- Publication date : 2001-07-16
Reference
Fadel MP, Szewczenko-Pawlikowski M, Leclerc P, Dziak E, Symonds JM, Blaschuk O, Michalak M, Opas M. Calreticulin affects beta-catenin-associated pathways. J. Biol. Chem. 2001;276:27083-9. doi: 10.1074/jbc.M101676200. PubMed PMID: 11369768.
Additional information
Keywords
animals base sequence calcium-binding proteins calreticulin cell adhesion cell line cytoskeletal proteins dna primers endoplasmic reticulum fibroblasts mice phosphorylation protein tyrosine phosphatases protein-tyrosine kinases reverse transcriptase polymerase chain reaction ribonucleoproteins signal transduction trans-activators tyrosine beta catenin
Abstract
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 beta-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.
