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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2005-2-9
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pubmed:abstractText |
COPII coat proteins are required for direct capture of cargo and SNARE proteins into transport vesicles from the endoplasmic reticulum (ER). Cargo and SNARE capture occurs during the formation of a 'prebudding complex' comprising a cargo, Sar1p-GTP and the COPII subunits Sec23/24p. The assembly and disassembly cycle of the prebudding complex on ER membranes is coupled to the Sar1p GTPase cycle. Using FRET to monitor a single round of Sec23/24p binding and dissociation from SNAREs in reconstituted liposomes, we show that Sec23/24p dissociates from v-SNARE and complexed t-SNARE with kinetics slower than Sar1p-GTP hydrolysis. Once Sec23/24p becomes associated with v-SNARE or complexed t-SNARE, the complex remains assembled during multiple rounds of Sar1p-GTP hydrolysis mediated by the GDP-GTP exchange factor Sec12p. These data suggest a model for the maintenance of kinetically stable prebudding complexes during the Sar1p GTPase cycle that regulates cargo sorting into transport vesicles.
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pubmed:commentsCorrections |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monomeric GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/SAR1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SEC12 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SEC23 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SEC24 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1545-9993
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
167-74
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15665868-COP-Coated Vesicles,
pubmed-meshheading:15665868-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:15665868-GTP Phosphohydrolases,
pubmed-meshheading:15665868-GTPase-Activating Proteins,
pubmed-meshheading:15665868-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:15665868-Guanosine Diphosphate,
pubmed-meshheading:15665868-Guanosine Triphosphate,
pubmed-meshheading:15665868-Hydrolysis,
pubmed-meshheading:15665868-Kinetics,
pubmed-meshheading:15665868-Liposomes,
pubmed-meshheading:15665868-Membrane Glycoproteins,
pubmed-meshheading:15665868-Membrane Proteins,
pubmed-meshheading:15665868-Monomeric GTP-Binding Proteins,
pubmed-meshheading:15665868-Protein Subunits,
pubmed-meshheading:15665868-Saccharomyces cerevisiae,
pubmed-meshheading:15665868-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:15665868-Time Factors,
pubmed-meshheading:15665868-Vesicular Transport Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis.
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pubmed:affiliation |
Molecular Membrane Biology Laboratory, RIKEN Discovery Research Institute, PRESTO, Japan Science and Technology Agency, Hirosawa, Wako, Saitama. kensato@riken.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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