The endoplasmic reticulum (ER) is the largest membrane-bound organelle in a typical eukaryotic cell. It consists of a continuous network of tubules and cisternae extending throughout the cytoplasm, with a total surface 0743-4634/89/1115-0001$02.00 PELHAM area at least six times that of the plasma membrane. Most of the ER membrane is studded with ribosomes (thus forming the rough endoplasmic reticulum, or RER). Membrane and secretory proteins are synthesized on these ribosomes and enter the ER, which is the starting point for the secretory pathway; such proteins spend only a short time in this organelle before being transported, by a process of vesicle budding and fusion, to the Golgi apparatus and thence to the cell surface (Palade 1975). The ER membrane and the lumen that it encloses also contain a characteristic set of resident proteins that are involved in the processing of secretory proteins and in other metabolic functions such as phospholipid biosynthesis. Thus, export of newly synthesized polypeptides from the ER involves the separaÂ tion of secretory proteins from resident proteins. In this article I discuss the mechanisms involved in this sorting process. Several other recent reviews have also covered this area (Pfeffer & Rothman 1 987; Rothman 1987;
Annual Review of Cell and Developmental Biology – Annual Reviews
Published: Nov 1, 1989
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