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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2006-11-19
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pubmed:databankReference |
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pubmed: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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
127
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
817-30
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pubmed:dateRevised |
2007-12-3
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pubmed:meshHeading |
pubmed-meshheading:17110339-Amino Acids,
pubmed-meshheading:17110339-Animals,
pubmed-meshheading:17110339-Membrane Proteins,
pubmed-meshheading:17110339-Mice,
pubmed-meshheading:17110339-Microscopy, Electron,
pubmed-meshheading:17110339-Models, Molecular,
pubmed-meshheading:17110339-Multiprotein Complexes,
pubmed-meshheading:17110339-Mutation,
pubmed-meshheading:17110339-Protein Binding,
pubmed-meshheading:17110339-Protein Structure, Secondary,
pubmed-meshheading:17110339-Protein Structure, Tertiary,
pubmed-meshheading:17110339-Protein Subunits,
pubmed-meshheading:17110339-Recombinant Proteins,
pubmed-meshheading:17110339-Saccharomyces cerevisiae,
pubmed-meshheading:17110339-Transport Vesicles,
pubmed-meshheading:17110339-Vesicular Transport Proteins
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pubmed:year |
2006
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pubmed:articleTitle |
The architecture of the multisubunit TRAPP I complex suggests a model for vesicle tethering.
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pubmed:affiliation |
Center for Biomolecular Recognition and Division of Molecular and Life Sciences, Department of Life Sciences, Pohang University of Science and Technology, Pohang, Kyungbuk 790-784, South Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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