RGD Reference Report - Localization of enolase in synaptic plasma membrane as an alphagamma heterodimer in rat brain. - Rat Genome Database

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Localization of enolase in synaptic plasma membrane as an alphagamma heterodimer in rat brain.

Authors: Ueta, H  Nagasawa, H  Oyabu-Manabe, Y  Toida, K  Ishimura, K  Hori, H 
Citation: Ueta H, etal., Neurosci Res. 2004 Apr;48(4):379-86.
RGD ID: 2302788
Pubmed: PMID:15041191   (View Abstract at PubMed)
DOI: DOI:10.1016/j.neures.2003.12.006   (Journal Full-text)

Enolase, a glycolytic enzyme, is a multifunctional protein with location diversity. We revealed the intracellular distribution of enolase isozymes, such as alphaalpha-, alphagamma- and gammagamma-enolases, in rat brain synaptic terminals by biochemical and immunoelectron microscopic analyses. Specific activity of enolase of synaptic plasma membrane fraction (SPM2) obtained from synaptosomes was 23.2 +/- 4.4 x 10(-2) micromol/mg protein/min in the presence of 0.25% Triton X-100 and that of synaptosomal cytoplasm (LS) was 67.4 +/- 12.1 x 10(-2) micromol/mg protein/min. About half of enolase activity in synaptosomes was distributed to soluble fraction while the remaining stayed in particulate membrane fractions by ultracentrifugation. Immunoblot analysis of the fractions demonstrated both alpha and gamma subunits were distributed in SPM. In addition, immunoelectron microscopic analysis also revealed that both subunits were immunoreactive on the SPM. Using coimmunoprecipitation assay, we confirmed that the enolase was present not only as a homodimer form but also as an alphagamma hybrid form associated with membrane, where both subunits were coimmunoprecipitated from lysate of SPM2 in the presence of Mg(2+). These findings indicate that all forms (alphaalpha, alphagamma, and gammagamma) of enolase translocate to the plasma membrane and associate with some components in the SPM.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
canonical glycolysis involved_inIDA 2302788; 2302788PMID:15041191CAFA 

Cellular Component
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
phosphopyruvate hydratase complex part_ofIDA 2302788; 2302788PMID:15041191CAFA 
synaptic membrane  IDA 2302788; 2302788 RGD 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
enzyme binding enablesIPIUniProtKB:P073232302788PMID:15041191CAFA 
enzyme binding enablesIPIUniProtKB:P047642302788PMID:15041191CAFA 
protein-containing complex binding  IDA 2302788; 2302788 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Eno1  (enolase 1)
Eno2  (enolase 2)


Additional Information