Linked Life Data

18249497

Source:http://linkedlifedata.com/resource/pubmed/id/18249497

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-2-29
pubmed:abstractText
Glutamate receptor (GluR) delta2 selectively expressed in cerebellar Purkinje cells (PCs) plays key roles in cerebellar long-term depression (LTD), motor learning and formation of parallel fiber (PF)-PC synapses. We have recently shown that the PDZ [postsynaptic density (PSD)-95/Discs large/zona occludens-1]-binding domain at the C-terminal, the T site, is essential for LTD induction and the regulation of climbing fiber (CF) territory, but is dispensable for synaptic localization of GluRdelta2, PF-PC synapse formation and CF elimination process. To investigate the functional roles of the S segment, the second PDZ-binding domain in the middle of the C-terminal cytoplasmic region, we generated GluRdelta2DeltaS mice carrying mutant GluRdelta2 lacking this segment. The amount of GluRdelta2DeltaS in mutant mice was reduced compared with that of GluRdelta2 in wild-type mice. However, the extent of decrease was much larger in the PSD fractions than in cerebellar homogenates, suggesting the requirement of the S segment for efficient synaptic localization. Furthermore, mismatched PF synapses and free spines emerged and CF-innervation territory on PC dendrites expanded in GluRdelta2DeltaS mice. On the other hand, the performance in the rotarod test was comparable between wild-type and GluRdelta2DeltaS mice. These results suggest that the S segment and T site, the two PDZ-binding domains in the C-terminal cytoplasmic region, are differentially involved in diverse GluRdelta2 functions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0304-3940
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
433
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
146-51
pubmed:meshHeading
pubmed-meshheading:18249497-Adaptor Proteins, Signal Transducing, pubmed-meshheading:18249497-Animals, pubmed-meshheading:18249497-Behavior, Animal, pubmed-meshheading:18249497-Calcium-Binding Protein, Vitamin D-Dependent, pubmed-meshheading:18249497-Cerebellum, pubmed-meshheading:18249497-Mice, pubmed-meshheading:18249497-Mice, Inbred C57BL, pubmed-meshheading:18249497-Mice, Transgenic, pubmed-meshheading:18249497-Microscopy, Electron, Transmission, pubmed-meshheading:18249497-Motor Activity, pubmed-meshheading:18249497-Mutation, pubmed-meshheading:18249497-Protein Binding, pubmed-meshheading:18249497-Protein Structure, Tertiary, pubmed-meshheading:18249497-Psychomotor Performance, pubmed-meshheading:18249497-Receptors, Glutamate, pubmed-meshheading:18249497-Synapses, pubmed-meshheading:18249497-Vesicular Glutamate Transport Protein 2
pubmed:year
2008
pubmed:articleTitle
Role of the internal Shank-binding segment of glutamate receptor delta2 in synaptic localization and cerebellar functions.
pubmed:affiliation
Department of Molecular Neurobiology and Pharmacology, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't