Receptor-mediated protein transport in the early secretory pathway

Trends Biochem Sci. 2007 Aug;32(8):381-8. doi: 10.1016/j.tibs.2007.06.006. Epub 2007 Jul 6.


Many secretory proteins are thought to rely upon transmembrane cargo receptors for efficient endoplasmic reticulum (ER)-to-Golgi transport. These receptors recognize specific cargo-encoded sorting signals. Only a few such cargo receptors have been characterized in detail, most of them in yeast. The only well-defined cargo receptor from mammalian cells, the LMAN1-MCFD2 complex, is required for the efficient secretion of coagulation factors V and VIII. Studies of this complex, coupled with recent advances in elucidating the basic machinery that mediates ER-to-Golgi transport, have provided a more-detailed picture of the mechanisms underlying receptor-mediated transport in the early secretory pathway. In addition to yeast studies, insights have also come from investigations into several inherited disorders that have recently been attributed to defects in the secretory pathway.

Publication types

  • Review

MeSH terms

  • Animals
  • COP-Coated Vesicles / metabolism
  • Caenorhabditis elegans
  • Cell Membrane / metabolism
  • Cytosol / metabolism
  • Drosophila melanogaster
  • Endoplasmic Reticulum / metabolism*
  • Fungal Proteins / chemistry
  • Golgi Apparatus / metabolism*
  • Humans
  • Mannose-Binding Lectins / metabolism
  • Membrane Proteins / metabolism
  • Protein Transport
  • Saccharomyces cerevisiae / metabolism
  • Vesicular Transport Proteins / metabolism


  • Fungal Proteins
  • LMAN1 protein, human
  • MCFD2 protein, human
  • Mannose-Binding Lectins
  • Membrane Proteins
  • Vesicular Transport Proteins