rdf:type |
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lifeskim:mentions |
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pubmed:issue |
31
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pubmed:dateCreated |
2004-8-5
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pubmed:abstractText |
Here, we show that postsynaptic p21-activated kinase (Pak) signaling diverges into two genetically separable pathways at the Drosophila neuromuscular junction. One pathway controls glutamate receptor abundance. Pak signaling within this pathway is specified by a required interaction with the adaptor protein Dreadlocks (Dock). We demonstrate that Dock is localized to the synapse via an Src homology 2-mediated protein interaction. Dock is not necessary for Pak localization but is necessary to restrict Pak signaling to control glutamate receptor abundance. A second genetically separable function of Pak kinase signaling controls muscle membrane specialization through the regulation of synaptic Discs-large. In this pathway, Dock is dispensable. We present a model in which divergent Pak signaling is able to coordinate two different features of postsynaptic maturation, receptor abundance, and muscle membrane specialization.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Glutamate,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/discs large 1 protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/dreadlocks protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/p21-Activated Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1529-2401
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pubmed:author |
|
pubmed:issnType |
Electronic
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pubmed:day |
4
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6871-9
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pubmed:dateRevised |
2007-11-19
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pubmed:meshHeading |
pubmed-meshheading:15295021-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:15295021-Animals,
pubmed-meshheading:15295021-Drosophila,
pubmed-meshheading:15295021-Drosophila Proteins,
pubmed-meshheading:15295021-GTP Phosphohydrolases,
pubmed-meshheading:15295021-Nerve Tissue Proteins,
pubmed-meshheading:15295021-Neuromuscular Junction,
pubmed-meshheading:15295021-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15295021-Receptors, Glutamate,
pubmed-meshheading:15295021-Synapses,
pubmed-meshheading:15295021-Synaptic Transmission,
pubmed-meshheading:15295021-Tumor Suppressor Proteins,
pubmed-meshheading:15295021-p21-Activated Kinases
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pubmed:year |
2004
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pubmed:articleTitle |
Coordinating structural and functional synapse development: postsynaptic p21-activated kinase independently specifies glutamate receptor abundance and postsynaptic morphology.
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pubmed:affiliation |
Department of Biochemistry and Biophysics, Program in Neuroscience, University of California, San Francisco, San Francisco, California 94143, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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