| Autor: |
Dascher C; Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92130, USA., Balch WE |
| Jazyk: |
angličtina |
| Zdroj: |
The Journal of biological chemistry [J Biol Chem] 1996 Jul 05; Vol. 271 (27), pp. 15866-9. |
| DOI: |
10.1074/jbc.271.27.15866 |
| Abstrakt: |
Members of the syntaxin gene family are components of protein complexes which regulate vesicle docking and/or fusion during transport of cargo through the secretory pathway of eukaryotic cells. We have previously demonstrated that syntaxin 5 is specifically required for endoplasmic reticulum to Golgi transport (Dascher, C., Matteson, J., and Balch, W. E.(1994) J. Biol. Chem. 269, 29363-29366). To extend these observations we have now cloned a protein from rat liver membranes which forms a native complex with syntaxin 5. We demonstrate that this protein is the mammalian homologue to yeast Sly1p, previously identified as a protein which genetically and biochemically interacts with the small GTPase Ypt1p and Sed5p, proteins involved in docking/fusion in the early secretory pathway of yeast. Using transient expression we find that overexpression of rat liver Sly1 (rSly1) can neutralize the dominant negative effects of excess syntaxin 5 on endoplasmic reticulum to Golgi transport. These results suggest that rSly1 functions to positively regulate syntaxin 5 function. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
