論文

査読有り
2002年12月

The postsynaptic density and dendritic raft localization of PSD-Zip70, which contains an N-myristoylation sequence and leucine-zipper motifs

JOURNAL OF CELL SCIENCE
  • D Konno
  • JA Kol
  • S Usui
  • K Hori
  • H Maruoka
  • M Inui
  • T Fujikado
  • Y Tano
  • T Suzuki
  • K Tohyama
  • K Sobue
  • 全て表示

115
23
開始ページ
4695
終了ページ
4706
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1242/jcs.00127
出版者・発行元
COMPANY OF BIOLOGISTS LTD

The postsynaptic site of the excitatory synapse, which is composed of the postsynaptic density (PSD) attached to the postsynaptic membrane, is a center for synaptic plasticity. To reveal the molecular organization and functional regulation of the postsynaptic site, we cloned a 70 kDa protein that is concentrated in PSDs using a monoclonal antibody against the PSD. This protein, named PSD-Zip70, is highly homologous to the human FEZ1/LZTS1 gene product. PSD-Zip70 contains an N-myristoylation consensus sequence, a polybasic cluster in the N-terminal region and four leucine-zipper motifs in the C-terminal region. Light and electron microscopy showed that this protein was localized to the dendritic spines, especially in the PSD and the postsynaptic membrane. Fractionation of the synaptic plasma membrane demonstrated that PSD-Zip70 was localized to the PSD and the dendritic raft. In Madin-Darby canine kidney (MDCK) cells, exogenous PSD-Zip70 was targeted to the apical plasma membrane of microvilli, and its N-myristoylation was necessary for this targeting. In hippocampal neurons, N-myristoylation was also required for the membrane localization and the C-terminal region was critically involved in the synaptic targeting. These results suggest that PSD-Zip70 may be involved in the dynamic properties of the structure and function of the postsynaptic site.

リンク情報
DOI
https://doi.org/10.1242/jcs.00127
CiNii Articles
http://ci.nii.ac.jp/naid/80015723008
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/12415013
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000179845400028&DestApp=WOS_CPL
ID情報
  • DOI : 10.1242/jcs.00127
  • ISSN : 0021-9533
  • CiNii Articles ID : 80015723008
  • PubMed ID : 12415013
  • Web of Science ID : WOS:000179845400028

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