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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1998-7-24
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pubmed:databankReference |
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pubmed:abstractText |
Phosphoinositides function as important second messengers in a wide range of cellular processes. Inositol polyphosphate 1-phosphatase (IPP) is an enzyme essential for the hydrolysis of the 1-phosphate from either Ins(1,4)P2 or Ins(1,3,4)P3. This enzyme is Li+ sensitive, and is one of the proposed targets of Li+ therapy in manic-depressive illness. Drosophila ipp mutants accumulate IP2 in their system and are incapable of metabolizing exogenous Ins(1,4)P2. Notably, ipp mutants demonstrate compensatory upregulation of an alternative branch in the inositol-phosphate metabolism tree, thus providing a means of ensuring continued availability of inositol. We demonstrate that ipp mutants have a defect in synaptic transmission resulting from a dramatic increase in the probability of vesicle release at larval neuromuscular junctions. We also show that Li+ phenocopies this effect in wild-type synapses. Together, these results support a role for phosphoinositides in synaptic vesicle function in vivo and mechanistically question the "lithium hypothesis."
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Lithium,
http://linkedlifedata.com/resource/pubmed/chemical/Neurotransmitter Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/inositol 1,3,4-trisphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/inositol 1,4-bis(phosphate),
http://linkedlifedata.com/resource/pubmed/chemical/inositol-1,4-bisphosphate...
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0896-6273
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1219-29
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9655509-Animals,
pubmed-meshheading:9655509-Chromosome Mapping,
pubmed-meshheading:9655509-Cloning, Molecular,
pubmed-meshheading:9655509-Drosophila,
pubmed-meshheading:9655509-Electrophysiology,
pubmed-meshheading:9655509-Female,
pubmed-meshheading:9655509-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:9655509-Inositol Phosphates,
pubmed-meshheading:9655509-Lithium,
pubmed-meshheading:9655509-Male,
pubmed-meshheading:9655509-Molecular Sequence Data,
pubmed-meshheading:9655509-Mutation,
pubmed-meshheading:9655509-Neurons,
pubmed-meshheading:9655509-Neurotransmitter Agents,
pubmed-meshheading:9655509-Phosphoric Monoester Hydrolases,
pubmed-meshheading:9655509-Sequence Homology, Amino Acid,
pubmed-meshheading:9655509-Substrate Specificity,
pubmed-meshheading:9655509-Synaptic Transmission,
pubmed-meshheading:9655509-Synaptic Vesicles
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pubmed:year |
1998
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pubmed:articleTitle |
Synaptic defects and compensatory regulation of inositol metabolism in inositol polyphosphate 1-phosphatase mutants.
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pubmed:affiliation |
Howard Hughes Medical Institute, and Department of Biology, University of California, San Diego, La Jolla 92093, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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