論文

査読有り 国際誌
2009年5月

Similar and distinct properties of MUPP1 and Patj, two homologous PDZ domain-containing tight-junction proteins.

Molecular and cellular biology
  • Makoto Adachi
  • ,
  • Yoko Hamazaki
  • ,
  • Yuka Kobayashi
  • ,
  • Masahiko Itoh
  • ,
  • Sachiko Tsukita
  • ,
  • Mikio Furuse
  • ,
  • Shoichiro Tsukita

29
9
開始ページ
2372
終了ページ
89
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1128/MCB.01505-08

MUPP1 and Patj are both composed of an L27 domain and multiple PDZ domains (13 and 10 domains, respectively) and are localized to tight junctions (TJs) in epithelial cells. Although Patj is known to be responsible for the organization of TJs and epithelial polarity, characterization of MUPP1 is lacking. In this study, we found that MUPP1 and Patj share several binding partners, including JAM1, ZO-3, Pals1, Par6, and nectins (cell-cell adhesion molecules at adherens junctions). MUPP1 and Patj exhibited similar subcellular distributions, and the mechanisms with which they localize to TJs also appear to overlap. Despite these similarities, functional studies have revealed that Patj is indispensable for the establishment of TJs and epithelial polarization, whereas MUPP1 is not. Thus, although MUPP1 and Patj share several molecular properties, their functions are entirely different. We present evidence that the signaling mediated by Pals1, which has a higher affinity for Patj than for MUPP1 and is involved in the activation of the Par6-aPKC complex, is of principal importance for the function of Patj in epithelial cells.

リンク情報
DOI
https://doi.org/10.1128/MCB.01505-08
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/19255144
PubMed Central
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2668367
ID情報
  • DOI : 10.1128/MCB.01505-08
  • PubMed ID : 19255144
  • PubMed Central 記事ID : PMC2668367

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