Signals for COPII-dependent export from the ER: what's the ticket out?

Trends Cell Biol. 2003 Jun;13(6):295-300. doi: 10.1016/s0962-8924(03)00082-5.

Abstract

Export of many secretory proteins from the endoplasmic reticulum (ER) relies on signal-mediated sorting into ER-derived transport vesicles. Recent work on the coat protein complex II (COPII) provides new insight into the mechanisms and signals that govern this selective export process. Conserved di-acidic and di-hydrophobic motifs found in specific transmembrane cargo proteins are required for their selection into COPII-coated vesicles. These signaling elements are cytoplasmically exposed and recognized by subunits of the COPII coat. Certain soluble cargo molecules depend on receptor-like proteins for efficient ER export, although signals that direct soluble cargo into ER-derived vesicles are less defined.

Publication types

  • Review

MeSH terms

  • Animals
  • COP-Coated Vesicles / metabolism*
  • Endoplasmic Reticulum / metabolism*
  • Humans
  • Protein Transport / physiology
  • Signal Transduction / physiology*