Article
Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin.
The Journal of biological chemistry - 27 Jan 2006
Martin Virginie, Groenendyk Jody, Steiner Simone S, Guo Lei, Dabrowska Monika, Parker J M Robert, Müller-Esterl Werner, Opas Michal, Michalak Marek
Abstract excerpt
Calreticulin is a Ca2+ -binding chaperone that resides in the lumen of the endoplasmic reticulum and is involved in the regulation of intracellular Ca2+ homeostasis and in the folding of newly synthesized glycoproteins. In this study, we have used site-specific mutagenesis to map amino acid residues that are critical in calreticulin function. We have focused on two cysteine residues (Cys(88) and Cys(120)), which...
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