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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Antibody specific for phosphorylated AMPA-type glutamate receptors at GluR2 Ser-696.

Possible phosphorylation sites on the Purkinje cell alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA)-type glutamate receptor subunits were identified using in vitro kinase assays of 17 synthetic peptides derived from the transmembrane-3 (TM3) domain to the end of C-terminal of a rat glutamate receptor 2 (GluR2). Only two peptides containing Ser-662 and Ser-696 were found to be efficiently phosphorylated by protein kinase C ( PKC). The peptide including Ser-696 was also phosphorylated by protein kinase G (PKG). Another peptide containing Thr-692 of a rat GluRA, clone almost identical to GluR1, was phosphorylated by PKC but not by PKG. Antisera recognizing phosphorylated AMPA receptor subunits at GluR2 Ser-696 or the homologous sites of GluR1/3/4 were produced, and the specificity of one of them, named 12P3, was established by enzyme-linked immunosorbent assay (ELISA), immunoblot and immunoprecipitation analyses. 12P3-immunocytochemistry on cerebellar slices demonstrated an AMPA-induced transient AMPA receptor phosphorylation, which appeared in Purkinje cell dendrites as well as somata immediately after AMPA treatment and disappeared after 20 min. This antibody may be a useful tool to study the role of AMPA receptor phosphorylation in producing synaptic plasticity.[1]

References

  1. Antibody specific for phosphorylated AMPA-type glutamate receptors at GluR2 Ser-696. Nakazawa, K., Tadakuma, T., Nokihara, K., Ito, M. Neurosci. Res. (1995) [Pubmed]
 
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