ELKS1 and Ca(2+) channel subunit β4 interact and colocalize at cerebellar synapses.
ELKS1 and Ca(2+) channel subunit β4 interact and colocalize at cerebellar synapses.
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DOI：
10.1097/wnr.0b013e32834e7deb
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发表时间：
2012-01-04
期刊：
影响因子：
1.7
通讯作者：
Nishimune H
中科院分区：
文献类型：
--
作者：
Billings SE;Clarke GL;Nishimune H
活性区的细胞骨架基质（CAZ）和突触电压依赖性钙通道（VDCC）都是组织和调节突触小泡释放的必要组成部分。在这里，我们报告了小脑分子层中 CAZ 蛋白 ELKS1b 和 VDCC 亚基 β4 之间的新相互作用。我们发现这两种蛋白质使用针对每种蛋白质的抗体进行共免疫沉淀。使用荧光免疫组织化学，我们观察到 ELKS1b 和 VDCC β4 在小脑分子层中的共定位，表明这些蛋白质都存在于分子层突触中。对 P/Q 型 VDCC 敲除小鼠 (Cacna1a−/−) 的分析表明，VDCC β4 亚基在分子层的定位被破坏，但 ELKS1b 蛋白的定位不受影响。结果表明，这两种蛋白质在体外相互作用并在小脑中共定位，并表明它们的相互作用可能在小脑的分子层突触中发挥作用。
The cytoskeletal matrix of the active zone (CAZ) and synaptic voltage-dependent calcium channels (VDCCs) are both necessary components for the organization and regulation of synaptic vesicle release. Here we report a novel interaction between the CAZ protein ELKS1b and the VDCC subunit β4 in the molecular layer of the cerebellum. We found that the two proteins co-immunoprecipitated using antibodies against each protein. Using fluorescent immunohistochemistry, we observed colocalization between ELKS1b and VDCC β4 in the molecular layer of the cerebellum, suggesting that these proteins are both present in molecular layer synapses. Analysis of a P/Q-type VDCC knockout mouse (Cacna1a−/−) revealed that the localization of the VDCC β4 subunit to the molecular layer was disrupted, although ELKS1b protein localization was not affected. The results demonstrate that these two proteins interact in vitro and colocalize in the cerebellum, and suggest that their interaction may play a role at the molecular layer synapses of the cerebellum.