![]() ![]() ERp57-dependent modulation of STAT3 is enhanced by complex formation between ERp57 and calreticulin. ![]() A model shows that ERp57, from the lumen of the ER, also affects STAT3 signaling and functions as a STAT3 inhibitor. ERp57 is also critical for MHC class I biosynthesis and assembly. For example, calnexin and calreticulin alternate binding between Glc 1 Man 9 GlcNAc 2 and Man 9 GlcNAc 2 protein-linked glycans to mediate substrate folding. ERp57 forms functional complexes with calnexin and calreticulin to promote protein folding, disulfide bond formation, and isomerization. This model shows cross-talk between ERp57, calreticulin, and STAT3 signaling. ERp57 catalyzes disulfide bond formation and isomerization within the glycoprotein substrate via a mixed disulfide intermediate involving a substrate cysteine (-SH) and cysteines within the active site CGHC motifs of ERp57 (-S-S-).97Ī model of the relationship between STAT3, ERp57, and calreticulin. 235 Citations Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum In vitro reconstitution of calreticulin-substrate. Details of the models are described in the text. Calnexin and calreticulin, which are lectin-type molecular chaperones, play important roles in glycoprotein folding. Mechanisms of calnexin and calreticulin action as described by the “lectin-only” and “dual-binding” models. Calnexin and calreticulin are related proteins that comprise an ER chaperone system that ensures the proper folding and quality control of newly synthesized glycoproteins. Use, when available, the link to Wikipedia (Es Trypsin)Įxternal links not available on Wikipedia have to be added here THE GENE Database A short protein description with the molecular wheight, isoforms, etc. ![]()
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