論文

査読有り
2003年3月

Synaptic targeting of PSD-Zip45 (Homer 1c) and its involvement in the synaptic accumulation of F-actin

JOURNAL OF BIOLOGICAL CHEMISTRY
  • S Usui
  • ,
  • D Konno
  • ,
  • K Hori
  • ,
  • H Maruoka
  • ,
  • S Okabe
  • ,
  • T Fujikado
  • ,
  • Y Tano
  • ,
  • K Sobue

278
12
開始ページ
10619
終了ページ
10628
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1074/jbc.M210802200
出版者・発行元
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

PSD-Zip45/Homer1c, which contains an enabled/VASP homology 1 (EVH1) domain and leucine zipper motifs, is a postsynaptic density (PSD) scaffold protein that interacts with metabotropic glutamate receptors and the shank family. We studied the molecular mechanism underlying the synaptic targeting of PSD-Zip45 in cultured hippocampal neurons. The EVH1 domain and the extreme C-terminal leucine zipper motif were molecular determinants for its synaptic targeting. The overexpression of the mutant of the EVH1 domain or deletion of the extreme C-terminal leucine zipper motif markedly suppressed the synaptic localization of endogenous shank but not PSD-95 or GKAP. In contrast, an overexpressed GKAP mutant lacking shank binding activity had no effect on the synaptic localization of shank. Actin depolymerization by latrunculin A reduced the synaptic localization of PSD-Zip45, shank, and F-actin but not of PSD-95 or GKAP. Overexpression of PSD-Zip45 enhanced the accumulation of synaptic F-actin. Additionally, overexpression. of PSD-Zip45 and an isoform of shank induced synaptic enlargement in association with the further accumulation of synaptic F-actin. The EVH1 domain and extreme C-terminal leucine zipper motif of PSD-Zip45 were also critical for these events. Thus, these data suggest that the PSD-Zip45-shank and PSD-95-GKAP complexes form different synaptic compartments, and PSD-Zip45 alone or PSD-Zip45-shank is involved in the synaptic accumulation of F-actin.

リンク情報
DOI
https://doi.org/10.1074/jbc.M210802200
CiNii Articles
http://ci.nii.ac.jp/naid/80015902474
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/12524440
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000181777500083&DestApp=WOS_CPL
ID情報
  • DOI : 10.1074/jbc.M210802200
  • ISSN : 0021-9258
  • CiNii Articles ID : 80015902474
  • PubMed ID : 12524440
  • Web of Science ID : WOS:000181777500083

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