The process of 'quality control' in the endoplasmic reticulum (ER) involves
a variety of mechanisms that collectively ensure that only correctly folde
d, assembled and modified proteins are transported along the secretory path
way. In contrast, nonnative proteins are retained and eventually targeted f
or degradation. Recent work provides the first structural insights into the
process of glycoprotein folding in the ER involving the lectin chaperones
calnexin and calreticulin. Underlying principles governing the choice of ch
aperone system engaged by different proteins have also been discovered.