首页> 外文期刊>Life sciences >Phosphorylation-dependent reversible translocation of Ca2+/calmodulin-dependent protein kinase II to the postsynaptic densities.
【24h】

Phosphorylation-dependent reversible translocation of Ca2+/calmodulin-dependent protein kinase II to the postsynaptic densities.

机译:Ca2 + /钙调蛋白依赖性蛋白激酶II磷酸化依赖性可逆转位至突触后密度。

获取原文
获取原文并翻译 | 示例
获取外文期刊封面目录资料

摘要

The translocation of soluble Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) to postsynaptic densities (PSDs) was investigated. When soluble CaM kinase II previously autophosphorylated was incubated with PSDs, the kinase was precipitated by centrifugation, indicating that the soluble kinase associated with PSDs and formed a PSD-CaM kinase II complex. Ca2+-independent activity generated by autophosphorylation of the kinase was retained in the complex. A number of PSD proteins were phosphorylated by the kinase associated with PSDs in both the absence and presence of Ca2+. When PSD-CaM kinase II complex was incubated at 30 degrees C, the enzyme was dephosphorylated and released from the complex. These results indicate that CaM kinase II reversibly translocates to PSDs in a phosphorylation-dependent manner.
机译:研究了可溶性Ca2 + /钙调蛋白依赖性蛋白激酶II(CaM激酶II)向突触后密度(PSDs)的易位。当将先前被自身磷酸化的可溶性CaM激酶II与PSDs孵育时,通过离心使该激酶沉淀,表明该可溶性激酶与PSD相关并形成了PSD-CaM激酶II复合物。通过激酶的自身磷酸化产生的Ca2 +非依赖性活性保留在复合物中。在不存在和存在Ca2 +的情况下,许多PSD蛋白都被与PSD相关的激酶磷酸化。当PSD-CaM激酶II复合物在30摄氏度下孵育时,酶被去磷酸化并从复合物中释放。这些结果表明,CaM激酶II以磷酸化依赖性方式可逆地转移至PSD。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号