Abstract
The lumen of the endoplasmic reticulum (ER) is a protein-folding compartment. Of course, protein folding occurs in other subcellular compartments but this is incidental to their other major functions. In the case of the lumen of the ER, protein folding comes close to being its raison d’être. Proteins entering this compartment do so cotranslationally (see Klappa et al. and Simon and Blobel, this volume) and in a physical state that is certainly not folded. Most models show them as extended Polypeptide chains but there is little real evidence to describe their physical properties at the point of translocation; it has been suggested (Bychkova et al., 1988) that the “translocation-competent” state is close to the “molten globule” or “collapsed intermediate” state described by students of protein refolding in vitro. On the other hand, proteins leaving the ER lumen, and proceeding to subsequent compartments of the secretory pathway, are usually fully folded, as judged by their biological activity and recognition by conformation-specific antibodies. Indeed, correct folding and assembly is the major criterion used by the “quality control” system that selectively permits exit of secretory and cell-surface proteins from the ER lumen (Hurtley and Helenius, 1989). Thus, proteins destined for secretion enter the lumen unfolded and leave folded and active.
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Rowling, P.J.E., Freedman, R.B. (1993). Folding, Assembly, and Posttranslational Modification of Proteins within the Lumen of the Endoplasmic Reticulum. In: Borgese, N., Harris, J.R. (eds) Endoplasmic Reticulum. Subcellular Biochemistry, vol 21. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2912-5_3
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