Abstract
The assembly of secreted and membrane proteins in the rough endoplasmic reticulum (RER) of eukaryotic cells is a complex process. As polypeptides are synthesized on membrane-bound ribosomes they are translocated across the RER membrane [1], the nascent potypeptide chains being modified as they emerge into the RER lumen. The N-terminal signal sequences are cleaved off by signal peptidase [2] and most nascent polypeptides are glycosylated on asparagine residues by oligosaccharyltransferase. The machinery required for the targeting of polypeptides to the RER membrane, namely the signal recognition particle and its membrane receptor, have been isolated and characterized. Much less is known, however, about the proteins involved in the later events of protein translocation-glycosylation and signal peptide cleavage.
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