Glycan-dependent and -independent interactions contribute to cellular substrate recruitment by calreticulin

Abstract

Background: We investigated the different modes of calreticulin-substrate binding. Results: Calreticulin binds glycosylated and nonglycosylated proteins with similar affinities but distinct kinetics and P-domain conformations. Conclusion: Successful substrate recruitment by calreticulin requires glycan and P-domain-dependent interactions. Significance: Elucidation of the distinct modes of calreticulin binding to substrate glycan and polypeptide components and their combined contributions to substrate recruitment in cells. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.