Postsynaptic Clustering and Activation of Pyk2 by PSD-95

被引:62
作者
Bartos, Jason A. [2 ]
Ulrich, Jason D. [2 ]
Li, Hongbin [3 ]
Beazely, Michael A. [3 ]
Chen, Yucui [2 ]
MacDonald, John F. [3 ,4 ]
Hell, Johannes W. [1 ,2 ]
机构
[1] Univ Calif Davis, Dept Pharmacol, Sch Med, Davis, CA 95616 USA
[2] Univ Iowa, Dept Pharmacol, Roy J & Lucille A Carver Coll Med, Iowa City, IA 52242 USA
[3] Univ Toronto, Dept Physiol, Toronto, ON M5S 1A8, Canada
[4] Univ Western Ontario, Robarts Res Inst, London, ON N6A 5K8, Canada
基金
加拿大健康研究院; 美国国家卫生研究院;
关键词
PROTEIN-TYROSINE KINASE; LONG-TERM POTENTIATION; D-ASPARTATE RECEPTOR; FOCAL ADHESION KINASE; VASCULAR SMOOTH-MUSCLE; MOSSY FIBER SYNAPSES; NEURONAL CELL-DEATH; NMDA RECEPTOR; HIPPOCAMPAL-NEURONS; EXCITATORY SYNAPSES;
D O I
10.1523/JNEUROSCI.4992-08.2010
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
The tyrosine kinase Pyk2 plays a unique role in intracellular signal transduction by linking Ca2+ influx to tyrosine phosphorylation, but the molecular mechanism of Pyk2 activation is unknown. We report that Pyk2 oligomerization by antibodies in vitro or overexpression of PSD-95 in PC6-3 cells induces trans-autophosphorylation of Tyr402, the first step in Pyk2 activation. In neurons, Ca2+ influx through NMDA-type glutamate receptors causes postsynaptic clustering and autophosphorylation of endogenous Pyk2 via Ca2+- and calmodulin-stimulated binding to PSD-95. Accordingly, Ca2+ influx promotes oligomerization and thereby autoactivation of Pyk2 by stimulating its interaction with PSD-95. We show that this mechanism of Pyk2 activation is critical for long-term potentiation in the hippocampus CA1 region, which is thought to underlie learning and memory.
引用
收藏
页码:449 / 463
页数:15
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