Syntaxin 9 is enriched in skin hair follicle epithelium and interacts with the epidermal growth factor receptor.
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.
Wang
Ya
Y
Department of Biochemistry, Yong Lou Lin School of Medicine, National University of Singapore, MD7, 8 Medical Drive, Singapore 117597.
Foo
Ling Yann
LY
Guo
Ke
K
Gan
Bin Qi
BQ
Zeng
Qi
Q
Hong
Wanjin
W
Tang
Bor Luen
BL
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D004247:DNA / Q000235:genetics; D004705:Endocytosis; D004847:Epithelial Cells / Q000378:metabolism; D066246:ErbB Receptors / Q000378:metabolism*; D018859:Hair Follicle / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D017403:In Situ Hybridization; D066298:In Vitro Techniques; D051379:Mice; D008969:Molecular Sequence Data; D050765:Qa-SNARE Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011990:Receptors, Transferrin / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D014018:Tissue Distribution
D050765:Qa-SNARE Proteins; D011990:Receptors, Transferrin; D011993:Recombinant Fusion Proteins; D004247:DNA; D066246:ErbB Receptors