Source:http://linkedlifedata.com/resource/pubmed/id/18066585
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2008-5-14
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pubmed:abstractText |
Trafficking of the intracellular vesicles and membrane protein incorporated in the vesicles is essential for a variety of basic biological processes. Growing evidence has highlighted the importance of the actin cytoskeleton in the trafficking of synaptic vesicles, secretory granules, transporters, and channels including aquaporin. These trafficking processes require actin remodeling, which is spatiotemporally regulated. Recent researches have come to focus on the motility mechanism of the translocation. In this review, we describe the role of actin at each step of intracellular reservation, exocytosis, docking, fusion with the plasma membrane, and endocytosis, focusing on aquaporin-2 trafficking.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Aquaporin 2,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Clathrin,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0031-6768
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
456
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
737-45
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pubmed:meshHeading |
pubmed-meshheading:18066585-Actins,
pubmed-meshheading:18066585-Animals,
pubmed-meshheading:18066585-Aquaporin 2,
pubmed-meshheading:18066585-Carrier Proteins,
pubmed-meshheading:18066585-Cell Fusion,
pubmed-meshheading:18066585-Clathrin,
pubmed-meshheading:18066585-Exocytosis,
pubmed-meshheading:18066585-Humans,
pubmed-meshheading:18066585-Ion Channels,
pubmed-meshheading:18066585-Transport Vesicles
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pubmed:year |
2008
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pubmed:articleTitle |
The role of actin remodeling in the trafficking of intracellular vesicles, transporters, and channels: focusing on aquaporin-2.
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pubmed:affiliation |
Department of Nephrology, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo, Japan. ynodmed2@tmd.ac.jp
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pubmed:publicationType |
Journal Article,
Review
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