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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2002-1-28
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pubmed:databankReference |
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pubmed:abstractText |
The small GTPase Rab family, which cycles between GTP-bound active and GDP-bound inactive states, plays an important role in membrane trafficking. Among them, Rab5 is involved in early endocytic pathway, and several Rab5-binding proteins have been identified as regulators or effectors to coordinate the docking and fusion processes of endocytic vesicles. We describe a novel binding protein exhibiting unique biochemical properties for Rab5. The Rab5-binding protein enhances GDP-GTP exchange reaction on Rab5 but preferentially interacts with its GTP-bound form. Gel filtration and immunoprecipitation analyses indicate that the Rab5-binding protein functions as a tetramer composed of anti-parallel linkage of two parallel dimers. These results suggest that the newly identified protein may function as an upstream activator and/or downstream effector for Rab5 in endocytic pathway. Possible roles of the quaternary structure have been discussed in terms of the Rab5-mediated signaling.
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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 |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3412-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11733506-Amino Acid Sequence,
pubmed-meshheading:11733506-Animals,
pubmed-meshheading:11733506-Binding Sites,
pubmed-meshheading:11733506-Blotting, Northern,
pubmed-meshheading:11733506-COS Cells,
pubmed-meshheading:11733506-Carrier Proteins,
pubmed-meshheading:11733506-Cercopithecus aethiops,
pubmed-meshheading:11733506-Cloning, Molecular,
pubmed-meshheading:11733506-Gene Library,
pubmed-meshheading:11733506-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:11733506-Guanosine 5'-O-(3-Thiotriphosphate),
pubmed-meshheading:11733506-Guanosine Diphosphate,
pubmed-meshheading:11733506-Guanosine Triphosphate,
pubmed-meshheading:11733506-HeLa Cells,
pubmed-meshheading:11733506-Humans,
pubmed-meshheading:11733506-Kinetics,
pubmed-meshheading:11733506-Leukocytes,
pubmed-meshheading:11733506-Molecular Sequence Data,
pubmed-meshheading:11733506-Recombinant Proteins,
pubmed-meshheading:11733506-Saccharomyces cerevisiae,
pubmed-meshheading:11733506-Sequence Alignment,
pubmed-meshheading:11733506-Sequence Homology, Amino Acid,
pubmed-meshheading:11733506-Transfection,
pubmed-meshheading:11733506-rab5 GTP-Binding Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
A novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTPase Rab5.
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pubmed:affiliation |
Department of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo 113-0033, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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