Phosphorylation-dependent interactions of α-Actinin-1/IQGAP1 with the AMPA receptor subunit GluR4

Mutsuo Nuriya, Sekyung Oh, Richard L. Huganir

研究成果: Article査読

31 被引用数 (Scopus)

抄録

AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid) receptors play key roles in excitatory synaptic transmission and synaptic plasticity in the CNS. Although a variety of proteins has been characterized to interact with AMPA receptors and regulate their function, little is known about the regulation of the AMPA receptor subunit GluR4. To understand the molecular mechanisms of GluR4 functional regulation, the yeast two-hybrid system was used to identify GluR4-interacting molecules. α-Actinin-1 and IQGAP1 were identified to be GluR4-specific binding partners. Both proteins interact specifically with GluR4 and co-cluster with GluR4 individually in neurons. Mapping experiments revealed that α-Actinin-1 and IQGAP1 bind to the same region within the C-terminus of GluR4 that contains a previously identified PKA phosphorylation site, Ser842, phosphorylation of which is regulated by synaptic activity. Interestingly, the phosphorylation of Ser842 differentially regulates interactions of GluR4 with α-Actinin-1 and IQGAP1; phosphorylation strongly inhibits interaction of GluR4 with α-Actinin-1 but has little effect on its interaction with IQGAP1. These results suggest that α-Actinin-1 and IQGAP1 regulate GluR4 functions via their specific associations with GluR4. In addition, our data indicate that activity-dependent phosphorylation of GluR4 may regulate its synaptic targeting through phosphorylation-dependent interactions with α-Actinin-1 and IQGAP1.

本文言語English
ページ(範囲)544-552
ページ数9
ジャーナルJournal of Neurochemistry
95
2
DOI
出版ステータスPublished - 2005 10月 1
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 細胞および分子神経科学

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