Related Experiment Video
Updated: Jun 1, 2026

Forward Genetic Screen Using Transgenic Calcium Reporter Aequorin to Identify Novel Targets in Calcium Signaling
Published on: August 1, 2020
Diverging functions among calreticulin isoforms in higher plants
Lisa Thelin1, Marek Mutwil, Marianne Sommarin
1Center for Molecular Protein Science, Biochemistry and Biophysical Chemistry, Lund University, Lund, Sweden.
Abstract:
The ER chaperone calreticulin plays vital roles in numerous cellular processes, including Ca2+-homeostasis, apoptosis, and cell adhesion, in animal cells. Although calreticulin has been systematically characterized in animal cells, the focus has been on one of the isoforms. However, recent advances in the plant calreticulin field have revealed functional divergence of calreticulin isoforms. While two of the plant isoforms appear to work within a general ER chaperone framework, the third isoform is associated with folding of receptors for brassinosteroids and bacterial peptides. Hence, the discovery of functional specialization of plant calreticulins opens up new vistas for calreticulins also in the animal field.
Related Concept Videos
Cell Signaling in Plants
Protein Folding Quality Check in the RER
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Calvin Benson Cycle
Cell Adhesion in Plants
Pectins are complex heteropolymers mainly composed of negatively-charged α-D-glucopyranosyl uronic acid and some neutral glycosyl residues such as α-L-rhamnopyranose, α-L-arabinofuranose, and...
Regulation of the Unfolded Protein Response
