Interaction between PAR-3 and the aPKC–PAR-6 complex is indispensable for apical domain development of epithelial cells
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- Yosuke Horikoshi
- Department of Molecular Biology, Yokohama City University Graduate School of Medical Science, 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236-0004, Japan
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- Atsushi Suzuki
- Department of Molecular Biology, Yokohama City University Graduate School of Medical Science, 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236-0004, Japan
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- Tomoyuki Yamanaka
- Department of Molecular Biology, Yokohama City University Graduate School of Medical Science, 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236-0004, Japan
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- Kazunori Sasaki
- Department of Molecular Biology, Yokohama City University Graduate School of Medical Science, 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236-0004, Japan
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- Keiko Mizuno
- Department of Molecular Biology, Yokohama City University Graduate School of Medical Science, 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236-0004, Japan
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- Hajime Sawada
- Department of Histology and Cell Biology, Yokohama City University Graduate School of Medical Science, 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236-0004, Japan
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- Shigenobu Yonemura
- Electron Microscope Laboratory, RIKEN Center for Developmental Biology, 2-2-3 Minatojima-minamimachi, Chuo-ku, Kobe 650-0047, Japan
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- Shigeo Ohno
- Department of Molecular Biology, Yokohama City University Graduate School of Medical Science, 3-9 Fuku-ura, Kanazawa-ku, Yokohama 236-0004, Japan
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説明
<jats:p>The evolutionarily conserved polarity proteins PAR-3, atypical protein kinase C (aPKC) and PAR-6 critically regulate the apical membrane development required for epithelial organ development. However, the molecular mechanisms underlying their roles remain to be clarified. We demonstrate that PAR-3 knockdown in MDCK cells retards apical protein delivery to the plasma membrane, and eventually leads to mislocalized apical domain formation at intercellular regions in both two-dimensional and three-dimensional culture systems. The defects in PAR-3 knockdown cells are efficiently rescued by wild-type PAR-3, but not by a point mutant (S827/829A) that lacks the ability to interact with aPKC, indicating that formation of the PAR-3–aPKC–PAR-6 complex is essential for apical membrane development. This is in sharp contrast with tight junction maturation, which does not necessarily depend on the aPKC–PAR-3 interaction, and indicates that the two fundamental processes essential for epithelial polarity are differentially regulated by these polarity proteins. Importantly, highly depolarized cells accumulate aPKC and PAR-6, but not PAR-3, on apical protein-containing vacuoles, which become targeted to PAR-3-positive primordial cell-cell contact sites during the initial stage of the repolarization process. Therefore, formation of the PAR-3–aPKC–PAR-6 complex might be required for targeting of not only the aPKC–PAR-6 complex but also of apical protein carrier vesicles to primordial junction structures.</jats:p>
収録刊行物
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- Journal of Cell Science
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Journal of Cell Science 122 (10), 1595-1606, 2009-05-15
The Company of Biologists
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キーワード
- Time Factors
- Cell Cycle Proteins
- Cell Communication
- Transfection
- Cell Line
- Tight Junctions
- Mice
- Dogs
- Animals
- Humans
- RNA, Small Interfering
- Protein Kinase C
- Adaptor Proteins, Signal Transducing
- Cysts
- Cell Membrane
- Cell Polarity
- Epithelial Cells
- beta Karyopherins
- Isoenzymes
- Protein Transport
- Mutation
- Vacuoles
- RNA Interference
- Collagen
- Cell Adhesion Molecules
- Gels
詳細情報 詳細情報について
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- CRID
- 1363951795075129216
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- ISSN
- 14779137
- 00219533
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- PubMed
- 19401335
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- データソース種別
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- Crossref
- OpenAIRE