The planar cell polarity protein Vangl2 is involved in postsynaptic compartmentalization

Tadahiro Nagaoka, Masashi Kishi

研究成果: Article

1 引用 (Scopus)

抄録

The excitatory postsynaptic region of the vertebrate hippocampus is usually compartmentalized into the postsynaptic density (PSD) and N-cadherin-rich domain, which is important for synaptic adhesion. However, the molecular mechanisms underlying the compartment formation are unknown. In the present report, we show that the planar cell polarity (PCP) protein Van Gogh-like 2 (Vangl2) plays a role in this regionalization. In cultured rat hippocampal neurons that were subjected to Vangl2 expression silencing, the formed clusters of PSD-95, one of the major scaffolding proteins in PSD, tended to overlap with those of N-cadherin. Further, in the dendrites of these neurons, the immunofluorescence of PSD-95 was to some extent diffused, without a significant change in the total signal. Because Vangl2 physically interacts with both PSD-95 and N-cadherin in vivo, these results suggest that a PCP-related direct molecular mechanism underlies the horizontal polarization of the postsynaptic regions.

元の言語English
ページ(範囲)251-255
ページ数5
ジャーナルNeuroscience Letters
612
DOI
出版物ステータスPublished - 26-01-2016
外部発表Yes

Fingerprint

Post-Synaptic Density
Cell Polarity
Cadherins
Proteins
Neurons
Dendrites
Fluorescent Antibody Technique
Vertebrates
Hippocampus

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)

これを引用

@article{e468d03d4f044e6fbc8d420fba3db4fd,
title = "The planar cell polarity protein Vangl2 is involved in postsynaptic compartmentalization",
abstract = "The excitatory postsynaptic region of the vertebrate hippocampus is usually compartmentalized into the postsynaptic density (PSD) and N-cadherin-rich domain, which is important for synaptic adhesion. However, the molecular mechanisms underlying the compartment formation are unknown. In the present report, we show that the planar cell polarity (PCP) protein Van Gogh-like 2 (Vangl2) plays a role in this regionalization. In cultured rat hippocampal neurons that were subjected to Vangl2 expression silencing, the formed clusters of PSD-95, one of the major scaffolding proteins in PSD, tended to overlap with those of N-cadherin. Further, in the dendrites of these neurons, the immunofluorescence of PSD-95 was to some extent diffused, without a significant change in the total signal. Because Vangl2 physically interacts with both PSD-95 and N-cadherin in vivo, these results suggest that a PCP-related direct molecular mechanism underlies the horizontal polarization of the postsynaptic regions.",
author = "Tadahiro Nagaoka and Masashi Kishi",
year = "2016",
month = "1",
day = "26",
doi = "10.1016/j.neulet.2015.12.009",
language = "English",
volume = "612",
pages = "251--255",
journal = "Neuroscience Letters",
issn = "0304-3940",
publisher = "Elsevier Ireland Ltd",

}

TY - JOUR

T1 - The planar cell polarity protein Vangl2 is involved in postsynaptic compartmentalization

AU - Nagaoka, Tadahiro

AU - Kishi, Masashi

PY - 2016/1/26

Y1 - 2016/1/26

N2 - The excitatory postsynaptic region of the vertebrate hippocampus is usually compartmentalized into the postsynaptic density (PSD) and N-cadherin-rich domain, which is important for synaptic adhesion. However, the molecular mechanisms underlying the compartment formation are unknown. In the present report, we show that the planar cell polarity (PCP) protein Van Gogh-like 2 (Vangl2) plays a role in this regionalization. In cultured rat hippocampal neurons that were subjected to Vangl2 expression silencing, the formed clusters of PSD-95, one of the major scaffolding proteins in PSD, tended to overlap with those of N-cadherin. Further, in the dendrites of these neurons, the immunofluorescence of PSD-95 was to some extent diffused, without a significant change in the total signal. Because Vangl2 physically interacts with both PSD-95 and N-cadherin in vivo, these results suggest that a PCP-related direct molecular mechanism underlies the horizontal polarization of the postsynaptic regions.

AB - The excitatory postsynaptic region of the vertebrate hippocampus is usually compartmentalized into the postsynaptic density (PSD) and N-cadherin-rich domain, which is important for synaptic adhesion. However, the molecular mechanisms underlying the compartment formation are unknown. In the present report, we show that the planar cell polarity (PCP) protein Van Gogh-like 2 (Vangl2) plays a role in this regionalization. In cultured rat hippocampal neurons that were subjected to Vangl2 expression silencing, the formed clusters of PSD-95, one of the major scaffolding proteins in PSD, tended to overlap with those of N-cadherin. Further, in the dendrites of these neurons, the immunofluorescence of PSD-95 was to some extent diffused, without a significant change in the total signal. Because Vangl2 physically interacts with both PSD-95 and N-cadherin in vivo, these results suggest that a PCP-related direct molecular mechanism underlies the horizontal polarization of the postsynaptic regions.

UR - http://www.scopus.com/inward/record.url?scp=84952673842&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84952673842&partnerID=8YFLogxK

U2 - 10.1016/j.neulet.2015.12.009

DO - 10.1016/j.neulet.2015.12.009

M3 - Article

VL - 612

SP - 251

EP - 255

JO - Neuroscience Letters

JF - Neuroscience Letters

SN - 0304-3940

ER -