Source:http://linkedlifedata.com/resource/pubmed/id/12853134
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
2003-7-10
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| pubmed:abstractText |
Vacuolar H(+)-ATPases (V-ATPases) are ATP-dependent proton pumps localized at membranes of intracellular acidic organelles and plasma membranes of various cell types. By virtue of its regulation in acidification, V-ATPase is required for many intracellular processes such as receptor-mediated endocytosis and protein sorting. Here we report the molecular characterization of the E subunit of V-ATPase in Caenorhabditis elegans. This subunit is one of the most well conserved subunits sharing approximately 57% identity with the human homologue, ATP6E. Green fluorescent protein (GFP) and whole-mount immunostaining analyses showed that V-ATPase E subunit (vha-8) is abundantly expressed in the H-shaped excretory cell, consistent with the expression patterns observed for other V-ATPase subunits. Double-stranded RNAs (or RNAi) targeted to vha-8 resulted in embryonic and larval lethality for the first filial generation, indicating that vha-8 is essential during early developmental processes. In addition, accumulation of abnormal endomitotic oocytes and defects in receptor-mediated endocytosis were observed in parental animals. These findings suggest that multiple phenotypes caused by the disruption of pH homeostasis are due to the defective V-ATPase. In summary, vha-8 encoding the E subunit of V-ATPase in C. elegans is essential for embryogenesis and receptor-mediated endocytosis.
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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/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Vacuolar Proton-Translocating...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jun
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| pubmed:issn |
0378-1119
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
5
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| pubmed:volume |
311
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
13-23
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:12853134-Amino Acid Sequence,
pubmed-meshheading:12853134-Animals,
pubmed-meshheading:12853134-Caenorhabditis elegans,
pubmed-meshheading:12853134-Egg Yolk,
pubmed-meshheading:12853134-Embryo, Nonmammalian,
pubmed-meshheading:12853134-Embryonic Development,
pubmed-meshheading:12853134-Female,
pubmed-meshheading:12853134-Gene Expression Regulation, Developmental,
pubmed-meshheading:12853134-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:12853134-Green Fluorescent Proteins,
pubmed-meshheading:12853134-Luminescent Proteins,
pubmed-meshheading:12853134-Male,
pubmed-meshheading:12853134-Microscopy, Fluorescence,
pubmed-meshheading:12853134-Microscopy, Immunoelectron,
pubmed-meshheading:12853134-Molecular Sequence Data,
pubmed-meshheading:12853134-Protein Subunits,
pubmed-meshheading:12853134-RNA Interference,
pubmed-meshheading:12853134-Recombinant Fusion Proteins,
pubmed-meshheading:12853134-Reproduction,
pubmed-meshheading:12853134-Sequence Homology, Amino Acid,
pubmed-meshheading:12853134-Vacuolar Proton-Translocating ATPases
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| pubmed:year |
2003
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| pubmed:articleTitle |
Vacuolar-type H+-ATPase E subunit is required for embryogenesis and yolk transfer in Caenorhabditis elegans.
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| pubmed:affiliation |
Department of Life Science, Kwangju Institute of Science and Technology (K-JIST), Kwangju 500-712, South Korea.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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