Autophosphorylation at Thr286 of the α calcium-calmodulin kinase II in LTP and learning
Autophosphorylation at Thr286 of the α calcium-calmodulin kinase II in LTP and learning
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DOI：
10.1126/science.279.5352.870
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发表时间：
1998-02-06
期刊：
影响因子：
56.9
通讯作者：
Silva, AJ
中科院分区：
文献类型：
--
作者：
Giese, KP;Fedorov, NB;Silva, AJ
钙-钙调蛋白依赖性激酶II（CaMKII）是海马长时程增强（LTP）和空间学习所必需的。除了其钙-钙调蛋白（CaM）依赖性活性外，CaMK II还可以进行自磷酸化，从而产生CaM非依赖性活性。在α CaMK Ⅱ基因中引入一个点突变，阻断该激酶286位苏氨酸的自磷酸化（Thr（286）），而不影响其CaM依赖性活性。突变小鼠在海马CAI区没有N-甲基-D-天冬氨酸受体依赖性LTP，在Morris水迷宫中没有空间学习能力。因此，在Thr（286）处的α CaMII的自磷酸化似乎是LTP和学习所需的。
The calcium-calmodulin-dependent kinase II (CaMKII) is required for hippocampal longterm potentiation (LTP) and spatial learning. In addition to its calcium-calmodulin (CaM)dependent activity, CaMKII can undergo autophosphorylation, resulting in CaM-independent activity. A point mutation was introduced into the alpha CaMKII gene that blocked the autophosphorylation of threonine at position 286 (Thr(286)) Of this kinase without affecting its CaM-dependent activity, The mutant mice had no N-methyl-D-aspartate receptor-dependent LTP in the hippocampal CAI area and showed no spatial learning in the Morris water maze. Thus, the autophosphorylation of alpha CaMII at Thr(286) appears to be required for LTP and learning.