| pubmed-article:19771148 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19771148 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:19771148 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:19771148 | lifeskim:mentions | umls-concept:C0205160 | lld:lifeskim |
| pubmed-article:19771148 | lifeskim:mentions | umls-concept:C0205396 | lld:lifeskim |
| pubmed-article:19771148 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:19771148 | lifeskim:mentions | umls-concept:C1710706 | lld:lifeskim |
| pubmed-article:19771148 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:19771148 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:19771148 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:19771148 | pubmed:dateCreated | 2009-9-22 | lld:pubmed |
| pubmed-article:19771148 | pubmed:abstractText | Presynaptic, electron-dense, cytoplasmic protrusions such as the T-bar (Drosophila) or ribbon (vertebrates) are believed to facilitate vesicle movement to the active zone (AZ) of synapses throughout the nervous system. The molecular composition of these structures including the T-bar and ribbon are largely unknown, as are the mechanisms that specify their synapse-specific assembly and distribution. In a large-scale, forward genetic screen, we have identified a mutation termed air traffic controller (atc) that causes T-bar-like protein aggregates to form abnormally in motoneuron axons. This mutation disrupts a gene that encodes for a serine-arginine protein kinase (SRPK79D). This mutant phenotype is specific to SRPK79D and is not secondary to impaired kinesin-dependent axonal transport. The srpk79D gene is neuronally expressed, and transgenic rescue experiments are consistent with SRPK79D kinase activity being necessary in neurons. The SRPK79D protein colocalizes with the T-bar-associated protein Bruchpilot (Brp) in both the axon and synapse. We propose that SRPK79D is a novel T-bar-associated protein kinase that represses T-bar assembly in peripheral axons, and that SRPK79D-dependent repression must be relieved to facilitate site-specific AZ assembly. Consistent with this model, overexpression of SRPK79D disrupts AZ-specific Brp organization and significantly impairs presynaptic neurotransmitter release. These data identify a novel AZ-associated protein kinase and reveal a new mechanism of negative regulation involved in AZ assembly. This mechanism could contribute to the speed and specificity with which AZs are assembled throughout the nervous system. | lld:pubmed |
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| pubmed-article:19771148 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19771148 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19771148 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19771148 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19771148 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19771148 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:19771148 | pubmed:issn | 1545-7885 | lld:pubmed |
| pubmed-article:19771148 | pubmed:author | pubmed-author:FetterRichard... | lld:pubmed |
| pubmed-article:19771148 | pubmed:author | pubmed-author:DavisGraeme... | lld:pubmed |
| pubmed-article:19771148 | pubmed:author | pubmed-author:JohnsonErvin... | lld:pubmed |
| pubmed-article:19771148 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19771148 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:19771148 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19771148 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19771148 | pubmed:pagination | e1000193 | lld:pubmed |
| pubmed-article:19771148 | pubmed:dateRevised | 2011-4-28 | lld:pubmed |
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