The architecture of the multisubunit TRAPP I complex suggests a model for vesicle tethering
SCIE
SCOPUS
- Title
- The architecture of the multisubunit TRAPP I complex suggests a model for vesicle tethering
- Authors
- Kim, YG; Raunser, S; Munger, C; Wagner, J; Song, YL; Cygler, M; Walz, T; Oh, BH; Sacher, M
- Date Issued
- 2006-11-17
- Publisher
- CELL PRESS
- Abstract
- Transport protein particle (TRAPP) 1 is a multi-subunit 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 1. 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 1 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.
- Keywords
- SPONDYLOEPIPHYSEAL DYSPLASIA-TARDA; TO-GOLGI TRANSPORT; CRYSTAL-STRUCTURE; MEMBRANE-FUSION; CIS-GOLGI; IDENTIFICATION; RECEPTOR; DOCKING; PROTEIN; BET3
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/23707
- DOI
- 10.1016/j.cell.2006.09.029
- ISSN
- 0092-8674
- Article Type
- Article
- Citation
- CELL, vol. 127, no. 4, page. 817 - 830, 2006-11-17
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- There are no files associated with this item.
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