CaMKII: A Molecular Substrate for Synaptic Plasticity and Memory

被引：103

作者：

Shonesy, Brian C. ^{[1
]}

Jalan-Sakrikar, Nidhi ^{[1
]}

Cavener, Victoria S. ^{[2
]}

Colbran, Roger J. ^{[1
,2
,3
]}

机构：

[1] Vanderbilt Univ, Sch Med, Dept Mol Physiol & Biophys, Nashville, TN 37212 USA

[2] Vanderbilt Univ, Sch Med, Vanderbilt Brain Inst, Nashville, TN 37212 USA

[3] Vanderbilt Univ, Sch Med, Vanderbilt Kennedy Ctr Res Human Dev, Nashville, TN 37212 USA

来源：

MOLECULAR BASIS OF MEMORY | 2014年 / 122卷

关键词：

PROTEIN-KINASE-II; LONG-TERM POTENTIATION; D-ASPARTATE RECEPTOR; ELEMENT-BINDING PROTEIN; ACTIVITY-DEPENDENT PHOSPHORYLATION; MICROTUBULE-ASSOCIATED PROTEIN-2; CALCIUM-INDEPENDENT ACTIVATION; POSTSYNAPTIC DENSITY FRACTION; SUBUNIT 2B NR2B; NMDA RECEPTOR;

D O I：

10.1016/B978-0-12-420170-5.00003-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Learning and memory is widely believed to result from changes in connectivity within neuronal circuits due to synaptic plasticity. Work over the past two decades has shown that Ca2+ influx during LTP induction triggers the activation of CaMKII in dendritic spines. CaMKII activation results in autophosphorylation of the kinase rendering it constitutively active long after the Ca2+ dissipates within the spine. This "molecular switch"(1) mechanism is essential for LTP and learning and memory. Here, we discuss this key regulatory mechanism and the diversity of downstream targets that can be modulated by CaMKII to exert dynamic control of synaptic structure and function.

引用

页码：61 / 87

页数：27

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