[HTML][HTML] Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle
T Soldà, N Garbi, GJ Hämmerling… - Journal of Biological …, 2006 - ASBMB
Members of the protein-disulfide isomerase superfamily catalyze the formation of intra-and
intermolecular disulfide bonds, a rate-limiting step of protein folding in the endoplasmic
reticulum (ER). Here we compared maturation of one obligate and two facultative calnexin
substrates in cells with and without ERp57, the calnexin-associated, glycoprotein-specific
oxidoreductase. ERp57 deletion did not prevent the formation of disulfide bonds during co-
translational translocation of nascent glycopolypeptides in the ER. It affected, however, the …
intermolecular disulfide bonds, a rate-limiting step of protein folding in the endoplasmic
reticulum (ER). Here we compared maturation of one obligate and two facultative calnexin
substrates in cells with and without ERp57, the calnexin-associated, glycoprotein-specific
oxidoreductase. ERp57 deletion did not prevent the formation of disulfide bonds during co-
translational translocation of nascent glycopolypeptides in the ER. It affected, however, the …
