Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2007-12-31
pubmed:abstractText
The V(0) complex forms the proteolipid pore of a vesicular ATPase that acidifies vesicles. In addition, an independent function in membrane fusion has been suggested in vacuolar fusion in yeast and synaptic vesicle exocytosis in fly neurons. Evidence for a direct role in secretion has also recently been presented in mouse and worm. The molecular mechanisms of how the V(0) components might act or are regulated are largely unknown. Here we report the identification and characterization of a calmodulin-binding site in the large cytosolic N-terminal region of the Drosophila protein V100, the neuron-specific V(0) subunit a1. V100 forms a tight complex with calmodulin in a Ca(2+)-dependent manner. Mutations in the calmodulin-binding site in Drosophila lead to a loss of calmodulin recruitment to synapses. Neuronal expression of a calmodulin-binding deficient V100 uncovers an incomplete rescue at low levels and cellular toxicity at high levels. Our results suggest a vesicular ATPase V(0)-dependent function of calmodulin at synapses.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
283
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
294-300
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:17933871-Amino Acid Sequence, pubmed-meshheading:17933871-Animals, pubmed-meshheading:17933871-Calcium, pubmed-meshheading:17933871-Calmodulin, pubmed-meshheading:17933871-Chromatography, Gel, pubmed-meshheading:17933871-Drosophila, pubmed-meshheading:17933871-Drosophila Proteins, pubmed-meshheading:17933871-Immunohistochemistry, pubmed-meshheading:17933871-Microscopy, Confocal, pubmed-meshheading:17933871-Molecular Sequence Data, pubmed-meshheading:17933871-Mutagenesis, pubmed-meshheading:17933871-Neurons, pubmed-meshheading:17933871-Photoreceptor Cells, Invertebrate, pubmed-meshheading:17933871-Protein Binding, pubmed-meshheading:17933871-Sequence Homology, Amino Acid, pubmed-meshheading:17933871-Synapses, pubmed-meshheading:17933871-Tryptophan, pubmed-meshheading:17933871-Vacuolar Proton-Translocating ATPases
pubmed:year
2008
pubmed:articleTitle
V-ATPase V0 sector subunit a1 in neurons is a target of calmodulin.
pubmed:affiliation
Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't