Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5574
pubmed:dateCreated
2002-6-7
pubmed:abstractText
The site of induction of long-term potentiation (LTP) at mossy fiber-CA3 synapses in the hippocampus is unresolved, with data supporting both pre- and postsynaptic mechanisms. Here we report that mossy fiber LTP was reduced by perfusion of postsynaptic neurons with peptides and antibodies that interfere with binding of EphB receptor tyrosine kinases (EphRs) to the PDZ protein GRIP. Mossy fiber LTP was also reduced by extracellular application of soluble forms of B-ephrins, which are normally membrane-anchored presynaptic ligands for the EphB receptors. The application of soluble ligands for presynaptic ephrins increased basal excitatory transmission and occluded both tetanus and forskolin-induced synaptic potentiation. These findings suggest that PDZ interactions in the postsynaptic neuron and trans-synaptic interactions between postsynaptic EphB receptors and presynaptic B-ephrins are necessary for the induction of mossy fiber LTP.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Ephrin-B1, http://linkedlifedata.com/resource/pubmed/chemical/Forskolin, http://linkedlifedata.com/resource/pubmed/chemical/Grip1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, EphA7, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, EphB2, http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, AMPA, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/glutamate receptor ionotropic...
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
7
pubmed:volume
296
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1864-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12052960-Adaptor Proteins, Signal Transducing, pubmed-meshheading:12052960-Amino Acid Motifs, pubmed-meshheading:12052960-Animals, pubmed-meshheading:12052960-Carrier Proteins, pubmed-meshheading:12052960-Cyclic AMP-Dependent Protein Kinases, pubmed-meshheading:12052960-Ephrin-B1, pubmed-meshheading:12052960-Excitatory Postsynaptic Potentials, pubmed-meshheading:12052960-Forskolin, pubmed-meshheading:12052960-Ligands, pubmed-meshheading:12052960-Long-Term Potentiation, pubmed-meshheading:12052960-Membrane Proteins, pubmed-meshheading:12052960-Mice, pubmed-meshheading:12052960-Mossy Fibers, Hippocampal, pubmed-meshheading:12052960-Nerve Tissue Proteins, pubmed-meshheading:12052960-Patch-Clamp Techniques, pubmed-meshheading:12052960-Peptide Fragments, pubmed-meshheading:12052960-Receptor, EphA7, pubmed-meshheading:12052960-Receptor, EphB2, pubmed-meshheading:12052960-Receptor Protein-Tyrosine Kinases, pubmed-meshheading:12052960-Receptors, AMPA, pubmed-meshheading:12052960-Recombinant Fusion Proteins, pubmed-meshheading:12052960-Signal Transduction, pubmed-meshheading:12052960-Synapses, pubmed-meshheading:12052960-Synaptic Transmission
pubmed:year
2002
pubmed:articleTitle
Trans-synaptic Eph receptor-ephrin signaling in hippocampal mossy fiber LTP.
pubmed:affiliation
Molecular Neurobiology Laboratory, The Salk Institute for Biological Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA. contractor@salk.edu
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't