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Binding of glutamate receptor delta2 to its scaffold protein, Delphilin, is regulated by PKA.

Biochem. Biophys. Res. Commun.2006 Nov 24;350(3):748-52. Epub 2006 Sep 28
Tomoko Sonoda 1 , Chieko Mochizuki , Tetsuji Yamashita , Keiko Watanabe-Kaneko , Yohei Miyagi , Yasushi Shigeri , Futoshi Yazama , Kenji Okuda , Susumu Kawamoto
Tomoko Sonoda 1 , Chieko Mochizuki , Tetsuji Yamashita , Keiko Watanabe-Kaneko , Yohei Miyagi , Yasushi Shigeri , Futoshi Yazama , Kenji Okuda , Susumu Kawamoto
+ et al

[No authors listed]

Author information
  • 1 Department of Molecular Biodefence Research, Yokohama City University Graduate School of Medicine, Yokohama, Japan.

摘要


The glutamate receptor delta2 (GluRdelta2) is selectively expressed in cerebellar Purkinje cells and plays an important role in motor learning, motor coordination, and long-term depression. Delphilin is identified as a GluRdelta2-interacting protein, selectively expressed in Purkinje cell-parallel fiber synapses, and specifically interacts with the GluRdelta2 C-terminus via its PDZ domain. Here, surface plasmon resonance analyses showed that Delphilin PDZ bound to GluRdelta2 C-terminal peptide (DPDRGTSI), but not to its phosphopeptides (DPDRGphosphoTSI and DPDRGTphosphoSI). We showed the incorporation of phosphate into threonine at -2 (-2T) and serine at -1 (-1S) of GluRdelta2 C-terminus by cAMP-dependent protein kinase in vitro. In the experiments using heterologous expression system, Delphilin coimmunoprecipitated with GluRdelta2 was dramatically decreased under the condition with forskolin and isobutylmethylxanthine, which led to cAMP-dependent phosphorylation by Thus, phosphorylation of -2T and/or -1S of GluRdelta2 C-terminus by may regulate the binding of GluRdelta2 to its scaffolding protein, Delphilin.