Syntaxin 9 is enriched in skin hair follicle epithelium and interacts with the epidermal growth factor receptor

Traffic. 2006 Feb;7(2):216-26. doi: 10.1111/j.1600-0854.2005.00378.x.


We describe a novel syntaxin family member, syntaxin 9 (Syn 9), which does not possess a typical C-terminal hydrophobic tail anchor. Syn 9 has, however, a Q-SNARE domain and an overall homology to syntaxins (with the highest overall homology with mammalian syntaxin 11). Syn 9 is enriched in some epithelial cells, particularly that of the stomach lining and the skin. At the skin, it is found in the epidermal layers as well as structures associated with hair follicles. A biochemical interaction screen revealed that Syn 9 interacts specifically with the epidermal growth factor (EGF) receptor. Overexpression of Syn 9 perturbed EGF receptor endocytosis but does not appear to affect the internalization of the transferrin receptor. Syn 9 may therefore have a role in EGF receptor transport and signaling in certain epithelial cell types.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Line
  • DNA / genetics
  • Endocytosis
  • Epithelial Cells / metabolism
  • ErbB Receptors / metabolism*
  • Hair Follicle / metabolism*
  • HeLa Cells
  • Humans
  • In Situ Hybridization
  • In Vitro Techniques
  • Mice
  • Molecular Sequence Data
  • Qa-SNARE Proteins / chemistry
  • Qa-SNARE Proteins / genetics
  • Qa-SNARE Proteins / metabolism*
  • Receptors, Transferrin / metabolism
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Signal Transduction
  • Tissue Distribution


  • Qa-SNARE Proteins
  • Receptors, Transferrin
  • Recombinant Fusion Proteins
  • DNA
  • ErbB Receptors