RGD Reference Report - SPIN90 dephosphorylation is required for cofilin-mediated actin depolymerization in NMDA-stimulated hippocampal neurons. - Rat Genome Database

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SPIN90 dephosphorylation is required for cofilin-mediated actin depolymerization in NMDA-stimulated hippocampal neurons.

Authors: Cho, IH  Lee, MJ  Kim, DH  Kim, B  Bae, J  Choi, KY  Kim, SM  Huh, YH  Lee, KH  Kim, CH  Song, WK 
Citation: Cho IH, etal., Cell Mol Life Sci. 2013 Nov;70(22):4369-83. doi: 10.1007/s00018-013-1391-4. Epub 2013 Jun 14.
RGD ID: 11570554
Pubmed: PMID:23765104   (View Abstract at PubMed)
PMCID: PMC3825632   (View Article at PubMed Central)
DOI: DOI:10.1007/s00018-013-1391-4   (Journal Full-text)

Actin plays a fundamental role in the regulation of spine morphology (both shrinkage and enlargement) upon synaptic activation. In particular, actin depolymerization is crucial for the spine shrinkage in NMDAR-mediated synaptic depression. Here, we define the role of SPIN90 phosphorylation/dephosphorylation in regulating actin depolymerization via modulation of cofilin activity. When neurons were treated with NMDA, SPIN90 was dephosphorylated by STEP61 (striatal-enriched protein tyrosine phosphatase) and translocated from the spines to the dendritic shafts. In addition, phosphorylated SPIN90 bound cofilin and then inhibited cofilin activity, suggesting that SPIN90 dephosphorylation is a prerequisite step for releasing cofilin so that cofilin can adequately sever actin filaments into monomeric form. We found that SPIN90 YE, a phosphomimetic mutant, remained in the spines after NMDAR activation where it bound cofilin, thereby effectively preventing actin depolymerization. This led to inhibition of the activity-dependent redistribution of cortactin and drebrin A, as well as of the morphological changes in the spines that underlie synaptic plasticity. These findings indicate that NMDA-induced SPIN90 dephosphorylation and translocation initiates cofilin-mediated actin dynamics and spine shrinkage within dendritic spines, thereby modulating synaptic activity.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Cfl1Ratcellular response to hydrogen peroxide  IDA  RGD 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Cfl1Ratprotein binding  IPINckipsd (Rattus norvegicus) RGD 
NckipsdRatprotein binding  IPICfl1 (Rattus norvegicus) RGD 

Objects Annotated

Genes (Rattus norvegicus)
Cfl1  (cofilin 1)
Nckipsd  (NCK interacting protein with SH3 domain)


Additional Information