| First Author | Kim YG | Year | 2006 |
| Journal | Cell | Volume | 127 |
| Issue | 4 | Pages | 817-30 |
| PubMed ID | 17110339 | Mgi Jnum | J:117477 |
| Mgi Id | MGI:3696594 | Doi | 10.1016/j.cell.2006.09.029 |
| Citation | Kim YG, et al. (2006) The architecture of the multisubunit TRAPP I complex suggests a model for vesicle tethering. Cell 127(4):817-30 |
| abstractText | Transport protein particle (TRAPP) I is a multisubunit vesicle tethering factor composed of seven subunits involved in ER-to-Golgi trafficking. The functional mechanism of the complex and how the subunits interact to form a functional unit are unknown. Here, we have used a multidisciplinary approach that includes X-ray crystallography, electron microscopy, biochemistry, and yeast genetics to elucidate the architecture of TRAPP I. The complex is organized through lateral juxtaposition of the subunits into a flat and elongated particle. We have also localized the site of guanine nucleotide exchange activity to a highly conserved surface encompassing several subunits. We propose that TRAPP I attaches to Golgi membranes with its large flat surface containing many highly conserved residues and forms a platform for protein-protein interactions. This study provides the most comprehensive view of a multisubunit vesicle tethering complex to date, based on which a model for the function of this complex, involving Rab1-GTP and long, coiled-coil tethers, is presented. |
