Source:http://linkedlifedata.com/resource/pubmed/id/18077461
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2008-2-11
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pubmed:abstractText |
The epithelial Ca(2+) channel TRPV5 plays an essential role in transcellular Ca(2+) transport and is one of the most Ca(2+)-selective members of the transient receptor potential superfamily. Regulation of the abundance of TRPV5 at the cell surface is critical in body Ca(2+) homeostasis. However, little is known about the mechanisms underlying TRPV5 endo- and exocytosis. Here, we show that TRPV5 is constitutively internalized in a dynamin- and clathrin-dependent manner. Internalized TRPV5 first appears in small vesicular structures and then localizes to perinuclear structures positive for Rab11a. TRPV5 has a half-life of more than 8 h and is stable even after internalization from the cell surface for more than 3 h. Disruption of cell surface delivery of newly synthesized TRPV5 by brefeldin A does not reduce TRPV5-mediated Ca(2+) influx in cells, suggesting the presence of a stable intracellular pool of the channel capable of recycling back to the surface. Furthermore, the endocytic recycling kinetics is decreased upon treatment with Ca(2+) chelator BAPTA-AM, indicating that the channel's trafficking pathways are dynamically controlled by Ca(2+).
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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/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Clathrin,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/TRPV Cation Channels,
http://linkedlifedata.com/resource/pubmed/chemical/TRPV5 protein, human
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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 | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4077-86
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pubmed:meshHeading |
pubmed-meshheading:18077461-Base Sequence,
pubmed-meshheading:18077461-Calcium,
pubmed-meshheading:18077461-Cell Line,
pubmed-meshheading:18077461-Clathrin,
pubmed-meshheading:18077461-DNA Primers,
pubmed-meshheading:18077461-Endocytosis,
pubmed-meshheading:18077461-Humans,
pubmed-meshheading:18077461-Mutagenesis, Site-Directed,
pubmed-meshheading:18077461-TRPV Cation Channels
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pubmed:year |
2008
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pubmed:articleTitle |
TRPV5 is internalized via clathrin-dependent endocytosis to enter a Ca2+-controlled recycling pathway.
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pubmed:affiliation |
Institute of Medical Biochemistry, Center for Molecular Biology of Inflammation, University of Münster, von-Esmarch-Strasse 56, Münster 48149, Germany. S.VandeGraaf-4@umcutrecht.nl
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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