Regulation of NMDA receptors by cyclin-dependent kinase-5

被引：207

作者：

Li, BS

Sun, MK

Zhang, L

Takahashi, S

Ma, W

Vinade, L

Kulkarni, AB

Brady, RO

Pant, HC

机构：

[1] NINCDS, Neurochem Lab, NIH, Bethesda, MD 20892 USA

[2] NINCDS, Lab Adapt Syst, NIH, Bethesda, MD 20892 USA

[3] NINCDS, Neurobiol Lab, NIH, Bethesda, MD 20892 USA

[4] NIMH, Behav Endocrinol Branch, NIH, Bethesda, MD 20892 USA

[5] Natl Inst Dent & Craniofacial Res, Funct Genom Unit, NIH, Bethesda, MD 20892 USA

[6] USN, Res Lab, Ctr Biomol Sci & Engn, Washington, DC 20375 USA

[7] NINCDS, Dev & Metab Neurol Branch, NIH, Bethesda, MD 20892 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2001年 / 98卷 / 22期

关键词：

D O I：

10.1073/pnas.211428098

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Members of the N-methyl-D-aspartate (NMDA) class of glutamate receptors (NMDARs) are critical for development, synaptic transmission, learning and memory; they are targets of pathological disorders in the central nervous system. NMDARs are phosphorylated by both serine/threonine and tyrosine kinases. Here, we demonstrate that cyclin dependent kinase-5 (Cdk5) associates with and phosphorylates NR2A subunits at Ser-1232 in vitro and in intact cells. Moreover, we show that roscovitine, a selective Cdk5 inhibitor, blocks both long-term potentiation induction and NMDA-evoked currents in rat CA1 hippocampal neurons. These results suggest that Cdk5 plays a key role in synaptic transmission and plasticity through its up-regulation of NMDARs.

引用

页码：12742 / 12747

页数：6

共 53 条

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