Article
Identification of an N-domain histidine essential for chaperone function in calreticulin.
The Journal of biological chemistry - 12 Dec 2003
Guo Lei, Groenendyk Jody, Papp Sylvia, Dabrowska Monika, Knoblach Barbara, Kay Cyril, Parker J M Robert, Opas Michal, Michalak Marek
Abstract excerpt
Calreticulin is an endoplasmic reticulum (ER) luminal Ca(2+)-binding chaperone involved in folding of newly synthesized glycoproteins via the "calreticulin-calnexin cycle." We reconstituted ER of calreticulin-deficient cells with N-terminal histidine (His25, His82, His128, and His153) calreticulin mutants and carried out a functional analysis. In crt(-/-) cells bradykinin-dependent Ca2+ release is altered, and...
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