Protein sorting receptors in the early secretory pathway

Abstract

Estimates based on proteomic analyses indicate that a third of translated proteins in eukaryotic genomes enter the secretory pathway. After folding and assembly of nascent secretory proteins in the endoplasmic reticulum (ER), the coat protein complex II (COPII) selects folded cargo for export in membrane-bound vesicles. To accommodate the great diversity in secretory cargo, protein sorting receptors are required in a number of instances for efficient ER export. These transmembrane sorting receptors couple specific secretory cargo to COPII through interactions with both cargo and coat subunits. After incorporation into COPII transport vesicles, protein sorting receptors release bound cargo in pre-Golgi or Golgi compartments, and receptors are then recycled back to the ER for additional rounds of cargo export. Distinct types of protein sorting receptors that recognize carbohydrate and/or polypeptide signals in secretory cargo have been characterized. Our current understanding of the molecular mechanisms underlying cargo receptor function are described.