期刊
FEBS LETTERS
卷 583, 期 22, 页码 3577-3581出版社
WILEY
DOI: 10.1016/j.febslet.2009.10.028
关键词
Phosphorylation; CaMKII; Ischemia
资金
- NIH [F31NS061584, T32GM007635, P30NS048154, R01NS052644]
CaMKII, a major mediator of synaptic plasticity, forms extra-synaptic clusters under ischemic conditions. This study further supports self-aggregation of CaMKII holoenzymes as the underlying mechanism. Aggregation in vitro was promoted by mimicking ischemic conditions: low pH (6.8 or less), Ca2+ (and calmodulin), and low ATP and/or high ADP concentration. Mutational analysis showed that high ATP prevented aggregation by a mechanism involving T286 auto-phosphorylation, and indicated requirement for nucleotide binding but not auto-phosphorylation also for extra-synaptic clustering within neurons. These results clarify a previously apparent paradox in the nucleotide and phosphorylation requirement of aggregation, and support a mechanism that involves inter-holoenzyme T286-region/T-site interaction. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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