Elaine F. Corbett

TL;DR: Calreticulin is a highly versatile lectin-like chaperone, and it participates during the synthesis of a variety of molecules, including ion channels, surface receptors, integrins and transporters.

TL;DR: Emerging evidence suggests that Ca2+ might also play a signaling role in the endoplasmic reticulum, and agonist-induced fluctuations in free Ca2+, which can affect many functions of the endoprotein synthesis and modification, and interchaperone interactions.

TL;DR: It is concluded that changes in ER lumenal Ca2+ concentration may be responsible for the regulation of protein-protein interactions via regulation of Ca2-dependent formation and maintenance of structural and functional complexes between different proteins involved in a variety of steps during protein synthesis, folding, and post-translational modification.

TL;DR: Ca(2+)-dependent changes in calreticulin's sensitivity to proteolysis indicate that agonist-induced fluctuation in the free ER luminal Ca(2+) concentration may affect the protein conformation and function.

TL;DR: Sera for anti‐CRT antibodies from patients with active and inactive systemic lupus ertythematosus and primary or secondary Sjögren’s syndrome were screened and limited proteolysis of CRT with two major leucocyte serine proteases demonstrated that an N‐terminal region ofCRT is resistant to digestion.