Competitive interaction of Seven in absentia homolog-1A and Ca2+/calmodulin with the cytoplasmic tail of group 1 metabotropic glutamate receptors

被引：73

作者：

Ishikawa, K ^{[1
]}

Nash, SR ^{[1
]}

Nishimune, A ^{[1
]}

Neki, A ^{[1
]}

Kaneko, S ^{[1
]}

Nakanishi, S ^{[1
]}

机构：

[1] Kyoto Univ, Fac Med, Dept Biol Sci, Sakyo Ku, Kyoto 6068501, Japan

来源：

GENES TO CELLS | 1999年 / 4卷 / 07期

关键词：

D O I：

10.1046/j.1365-2443.1999.00269.x

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Background: Group 1 metabotropic glutamate receptors (mGluR1 and mGluR5) are coupled to inositol trisphosphate/Ca2+ signaling via G proteins and play an important role in excitatory synaptic transmission, To explore the regulation of group 1 mGluR function, we applied the yeast two-hybrid system using the intracellular carboxy-terminal domain of group 1 mGluRs (group 1 ct-mGluRs) and attempted to identify novel protein-protein interactions of group 1 mGluRs. Results: The two-hybrid screening revealed a specific interaction between group 1 ct-mGluRs and Siah-1A, the mammalian homolog of Drosophila seven in absentia which is involved in photoreceptor cell differentiation via the ubiquitin/proteasome-dependent mechanism, This interaction occurs within a homologous 27-28 amino acid stretch within group 1 ct-mGluRs and requires the latter two-thirds of Siah-1A, Following coexpression in COS-7 cells, myc-tagged Siah-1A was coimmuno-precipitated with the flag-tagged ct-mGluRs by anti-flag antibody, Furthermore, in vitro binding revealed that Siah-1A and Ca2+/calmodulin (CaM) binding sites overlap, such that Siah-1A binding is competitively inhibited by CaM in a Ca2+-dependent manner. Conclusions: The results demonstrate a direct interaction between group 1 mGluRs and Siah-1A and suggest a novel modulatory mechanism mediated by a competitive interaction between Ca2+/CaM and Siah-1A.

引用

页码：381 / 390

页数：10

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