Recent data on the structural and molecular organisation of the endoplasmic reticulum (ER) are reviewed. A special attention is paid to the mechanism of soluble and integral membrane protein translocation across the ER bilayer. A model of phospholipid-coupled polypeptide translocation is introduced served to overcome hydrophobic and (or) conformational constraints during the passage of polar amino acid residues within a polar environment of the ER membrane. In addition the mechanisms of diverse covalent and noncovalent post-translocational polypeptide modifications are considered, together with the process of the sorting events among ER-resident polypeptides and those destined to leave the ER domain for the Golgi apparatus.
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