Stx5-Mediated ER-Golgi Transport in Mammals and Yeast

Cells. 2019 Jul 26;8(8):780. doi: 10.3390/cells8080780.


The soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) syntaxin 5 (Stx5) in mammals and its ortholog Sed5p in Saccharomyces cerevisiae mediate anterograde and retrograde endoplasmic reticulum (ER)-Golgi trafficking. Stx5 and Sed5p are structurally highly conserved and are both regulated by interactions with other ER-Golgi SNARE proteins, the Sec1/Munc18-like protein Scfd1/Sly1p and the membrane tethering complexes COG, p115, and GM130. Despite these similarities, yeast Sed5p and mammalian Stx5 are differently recruited to COPII-coated vesicles, and Stx5 interacts with the microtubular cytoskeleton, whereas Sed5p does not. In this review, we argue that these different Stx5 interactions contribute to structural differences in ER-Golgi transport between mammalian and yeast cells. Insight into the function of Stx5 is important given its essential role in the secretory pathway of eukaryotic cells and its involvement in infections and neurodegenerative diseases.

Keywords: Golgi apparatus; endoplasmic reticulum; membrane trafficking; secretory pathway; syntaxin 5.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Endoplasmic Reticulum / metabolism*
  • Golgi Apparatus / metabolism*
  • Humans
  • Intracellular Space / metabolism
  • Mammals
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Protein Isoforms / metabolism
  • Protein Multimerization
  • Protein Processing, Post-Translational
  • Protein Transport
  • Qa-SNARE Proteins / chemistry
  • Qa-SNARE Proteins / metabolism*
  • SNARE Proteins / metabolism
  • Structure-Activity Relationship
  • Vesicular Transport Proteins / metabolism
  • Yeasts


  • Protein Isoforms
  • Qa-SNARE Proteins
  • SNARE Proteins
  • Vesicular Transport Proteins