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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 |
2005-3-30
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pubmed:abstractText |
Application of Clostridium difficile toxin B, an inhibitor of the Rho family of GTPases, at the Aplysia sensory to motor neuron synapse blocks long-term facilitation and the associated growth of new sensory neuron varicosities induced by repeated pulses of serotonin (5-HT). We have isolated cDNAs encoding Aplysia Rho, Rac, and Cdc42 and found that Rho and Rac had no effect but that overexpression in sensory neurons of a dominant-negative mutant of ApCdc42 or the CRIB domains of its downstream effectors PAK and N-WASP selectively reduces the long-term changes in synaptic strength and structure. FRET analysis indicates that 5-HT activates ApCdc42 in a subset of varicosities contacting the postsynaptic motor neuron and that this activation is dependent on the PI3K and PLC signaling pathways. The 5-HT-induced activation of ApCdc42 initiates reorganization of the presynaptic actin network leading to the outgrowth of filopodia, some of which are morphological precursors for the learning-related formation of new sensory neuron varicosities.
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pubmed:grant |
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Serotonin,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Wiskott-Aldrich Syndrome Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/cdc42 GTP-Binding Protein,
http://linkedlifedata.com/resource/pubmed/chemical/p21-Activated Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/rac GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rho GTP-Binding Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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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:day |
24
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pubmed:volume |
45
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
887-901
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15797550-Actin Cytoskeleton,
pubmed-meshheading:15797550-Actins,
pubmed-meshheading:15797550-Amino Acid Sequence,
pubmed-meshheading:15797550-Animals,
pubmed-meshheading:15797550-Aplysia,
pubmed-meshheading:15797550-Cells, Cultured,
pubmed-meshheading:15797550-Conserved Sequence,
pubmed-meshheading:15797550-Learning,
pubmed-meshheading:15797550-Molecular Sequence Data,
pubmed-meshheading:15797550-Motor Neurons,
pubmed-meshheading:15797550-Mutation,
pubmed-meshheading:15797550-Nerve Tissue Proteins,
pubmed-meshheading:15797550-Neuronal Plasticity,
pubmed-meshheading:15797550-Neurons, Afferent,
pubmed-meshheading:15797550-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:15797550-Presynaptic Terminals,
pubmed-meshheading:15797550-Protein Structure, Tertiary,
pubmed-meshheading:15797550-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15797550-Pseudopodia,
pubmed-meshheading:15797550-Serotonin,
pubmed-meshheading:15797550-Synapses,
pubmed-meshheading:15797550-Type C Phospholipases,
pubmed-meshheading:15797550-Wiskott-Aldrich Syndrome Protein, Neuronal,
pubmed-meshheading:15797550-cdc42 GTP-Binding Protein,
pubmed-meshheading:15797550-p21-Activated Kinases,
pubmed-meshheading:15797550-rac GTP-Binding Proteins,
pubmed-meshheading:15797550-rho GTP-Binding Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
Serotonin-induced regulation of the actin network for learning-related synaptic growth requires Cdc42, N-WASP, and PAK in Aplysia sensory neurons.
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pubmed:affiliation |
Center for Neurobiology and Behavior, College of Physicians and Surgeons, Columbia University, New York, New York 10032, 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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