Abstract
In eukaryotic cells, secretory and plasma membrane proteins fold and oligomerize in the endoplasmic reticulum (ER) with the assistance of molecular chaperones. Such chaperones prevent inappropriate interactions between folding intermediates. Folding and oligomerization are prerequisites for exit from the ER and, for many proteins, exit from the ER is the limiting step for transport to the cell surface. Some ER chaperones such as BiP interact with many substrate proteins, whereas others, for example tapasin, promote assembly of a single protein complex. The function and physiological substrates of one of the most abundant ER chaperones, the Hsp90 orthologue gp96 (glycoprotein of 96 kDa), also known as Grp94 (glucose-regulated protein of 94 kDa), were ill-defined until now.
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