Assembly, sorting, and exit of oligomeric proteins from the endoplasmic reticulum

✍ Scribed by Padmalatha S. Reddy; Ronald B. Corley

• Publisher: John Wiley and Sons
• Year: 1998
• Tongue: English
• Weight: 135 KB
• Volume: 20
• Category: Article
• ISSN: 0265-9247
• DOI: 10.1002/(sici)1521-1878(199807)20:7<546::aid-bies5>3.0.co;2-i

✦ Synopsis

The endoplasmic reticulum (ER) uses various mechanisms to ensure that only properly folded proteins enter the secretory pathway. For proteins that oligomerize in the ER, the proper tertiary and quaternary structures must be achieved before their release. Although some proteins fold before oligomerization, others initiate oligomerization cotranslationally. Here, we discuss these different strategies and some of the unique problems they present for the ER quality control system. One mechanism used by the ER is thiol retention. Thiol retention operates by monitoring the redox state of specific cysteine residue(s) and was discovered in studies on the assembly of IgM, a complex oligomeric glycoprotein. This system is also involved in retaining other unassembled proteins in the ER. Mutations that result in uneven numbers of cysteine residues can subject yet other proteins to thiol retention, altering their oligomerization status and function. The implications of these results on the effects of thiol retention on protein function and cell fate are discussed.