RGD Reference Report - NMDA receptor-dependent synaptic translocation of insulin receptor substrate p53 via protein kinase C signaling. - Rat Genome Database

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NMDA receptor-dependent synaptic translocation of insulin receptor substrate p53 via protein kinase C signaling.

Authors: Hori, K  Yasuda, H  Konno, D  Maruoka, H  Tsumoto, T  Sobue, K 
Citation: Hori K, etal., J Neurosci. 2005 Mar 9;25(10):2670-81.
RGD ID: 9684984
Pubmed: PMID:15758177   (View Abstract at PubMed)
PMCID: PMC6725157   (View Article at PubMed Central)
DOI: DOI:10.1523/JNEUROSCI.3638-04.2005   (Journal Full-text)

The activity-dependent remodeling of postsynaptic structure is a fundamental process underlying learning and memory. Insulin receptor substrate p53 (IRSp53), a key player in cytoskeletal dynamics, is enriched in the postsynaptic density (PSD) fraction, but its significance in synaptic functions remains unclear. We report here that IRSp53 is accumulated rapidly at the postsynaptic sites of cultured hippocampal neurons after glutamate or NMDA stimulation in an actin cytoskeleton-dependent manner. Pharmacological profiles showed that a PKC inhibitor, but not other kinase inhibitors, specifically suppressed the synaptic translocation of IRSp53 in response to NMDA, and the selective activation of PKC with phorbol ester markedly induced the synaptic translocation. Reverse transcriptase-PCR and Western blotting showed that IRSp53-S is the major isoform expressed in cultured hippocampal neurons. The synaptic targeting of IRSp53-S was found to be mediated through N-terminal coiled-coil domain and the PDZ (PSD-95/Discs large/zona occludens-1)-binding sequence at its C-terminal end and regulated by the PKC phosphorylation of its N terminus. In electrophysiological experiments, overexpression of IRSp53-S wild type and IRSp53-S mutant that is spontaneously accumulated at the postsynaptic sites enhanced the postsynaptic function as detected by an increased miniature EPSC amplitude. These data suggest that IRSp53 is involved in NMDA receptor-linked synaptic plasticity via PKC signaling.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Baiap2Ratcellular response to L-glutamate  IEP  RGD 
Baiap2Ratpositive regulation of excitatory postsynaptic potential  IMP  RGD 
Baiap2Ratprotein localization to synapse  IMP  RGD 

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Baiap2Ratdendritic spine  IDA  RGD 
Baiap2Ratneuronal cell body  IDA  RGD 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Baiap2Ratscaffold protein binding  IPIRGD:68424 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Baiap2  (BAR/IMD domain containing adaptor protein 2)


Additional Information