Organization of the core structure of the postsynaptic density

被引：201

作者：

Chen, Xiaobing ^{[1
]}

Winters, Christine ^{[1
]}

Azzam, Rita

Li, Xiang ^{[3
]}

Galbraith, James A. ^{[1
]}

Leapman, Richard D. ^{[2
]}

Reese, Thomas S. ^{[1
]}

机构：

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

[2] Natl Inst Biomed Imaging & BioEngn, Lab Bioengn & Physical Sci, NIH, Bethesda, MD 20892 USA

[3] Columbia Univ, Dept Physiol & Cell Biophys, New York, NY 10032 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2008年 / 105卷 / 11期

关键词：

EM tomography; high-pressure freezing; hippocampal neuron; PSD-95;

D O I：

10.1073/pnas.0800897105

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：

Much is known about the composition and function of the postsynaptic density (PSD), but less is known about its molecular organization. We use EM tomography to delineate the organization of PSDs at glutamatergic synapses in rat hippocampal cultures. The core of the PSD is dominated by vertically oriented filaments, and ImmunoGold labeling shows that PSD-95 is a component of these filaments. Vertical filaments contact two types of transmembrane structures whose sizes and positions match those of glutamate receptors and intermesh with two types of horizontally oriented filaments lying 10-20 nm from the postsynaptic membrane. The longer horizontal filaments link adjacent NMDAR-type structures, whereas the smaller filaments link both NMDA- and AMPAR-type structures. The orthogonal, interlinked scaffold of filaments at the core of the PSD provides a structural basis for understanding dynamic aspects of postsynaptic function.

引用

页码：4453 / 4458

页数：6

共 47 条

[21] DOMAIN INTERACTION BETWEEN NMDA RECEPTOR SUBUNITS AND THE POSTSYNAPTIC DENSITY PROTEIN PSD-95 [J].