Source:http://linkedlifedata.com/resource/pubmed/id/18843259
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2009-1-16
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| pubmed:abstractText |
Trafficking of the water channel aquaporin-2 to the apical plasma membrane of the collecting duct is mediated by arginine vasopressin, rendering the cell permeable to water. We recently identified a novel form of aquaporin-2 that is phosphorylated at serine-269 (pS269-AQP2). Using antibodies specific for this form of the water channel, we detected rat and mouse pS269-AQP2 in the connecting tubule and throughout the collecting duct system. Using confocal immunofluorescence microscopy with organelle-specific markers and immunogold electron microscopy, we found that pS269-AQP2 was found only on the apical plasma membrane of principal cells. In vasopressin-deficient Brattleboro rats, pS269-AQP2 was undetectable but dramatically increased in abundance after these rats were treated with [deamino-Cys-1, d-Arg-8]vasopressin (dDAVP). This increase occurred only at the apical plasma membrane, even after long-term dDAVP treatment. Following dDAVP there was a time-dependent redistribution of total aquaporin-2 from predominantly intracellular vesicles to the apical plasma membrane, clathrin-coated vesicles, early endosomal compartments, and lysosomes. However, pS269-AQP2 was found only on the apical plasma membrane at any time. Our results show that S269 phosphorylated aquaporin-2 is exclusively associated with the apical plasma membrane, where it escapes endocytosis to remain at the cell surface.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
1523-1755
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
75
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
295-303
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| pubmed:dateRevised |
2011-9-26
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| pubmed:meshHeading |
pubmed-meshheading:18843259-Animals,
pubmed-meshheading:18843259-Aquaporin 2,
pubmed-meshheading:18843259-Cell Membrane,
pubmed-meshheading:18843259-Clathrin-Coated Vesicles,
pubmed-meshheading:18843259-Deamino Arginine Vasopressin,
pubmed-meshheading:18843259-Endosomes,
pubmed-meshheading:18843259-Immunohistochemistry,
pubmed-meshheading:18843259-Kidney Tubules, Collecting,
pubmed-meshheading:18843259-Lysosomes,
pubmed-meshheading:18843259-Mice,
pubmed-meshheading:18843259-Mice, Inbred C57BL,
pubmed-meshheading:18843259-Mice, Knockout,
pubmed-meshheading:18843259-Peroxidase,
pubmed-meshheading:18843259-Phosphorylation,
pubmed-meshheading:18843259-Rats,
pubmed-meshheading:18843259-Rats, Brattleboro,
pubmed-meshheading:18843259-Rats, Wistar,
pubmed-meshheading:18843259-Sensitivity and Specificity,
pubmed-meshheading:18843259-Serine,
pubmed-meshheading:18843259-Time Factors
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| pubmed:year |
2009
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| pubmed:articleTitle |
Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells.
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| pubmed:affiliation |
The Water and Salt Research Center, Institute of Anatomy, University of Aarhus, Aarhus, Denmark.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|