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Cited by 306Protein Kinase Regulation and GTPase SignalingDevelopmental Biology and Gene RegulationCellular Mechanics and Interactions

The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.

PAR‐6 regulates aPKC activity in a novel way and mediates cell‐cell contact‐induced formation of the epithelial junctional complex

Yamanaka, Tomoyuki, Horikoshi, Yosuke, Suzuki, Atsushi, Sugiyama, Yuki, Kitamura, Koichi, Maniwa, Rika, Nagai, Yoko, Yamashita, Akio, Hirose, Tomonori, Ishikawa, Hiroko, Ohno, Shigeo·2001·Genes to Cells
DOI 10.1046/j.1365-2443.2001.00453.x
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Abstract

Background PAR‐6, aPKC and PAR‐3 are polarity proteins that co‐operate in the establishment of cell polarity in Caenorhabditis elegans and Drosophila embryos. We have recently shown that mammalian aPKC is required for the formation of the epithelia‐specific cell‐cell junctional structure. We have also revealed that a mammalian PAR‐6 forms a ternary complex with aPKC and ASIP/PAR‐3, and localizes at the most apical end of the junctional complex in epithelial cells . Results The ternary complex formation and junctional co‐localization of PAR‐6 with aPKC and ASIP/PAR‐3 are observed during the early stage of epithelial cell polarization. In addition, over‐expression of the PAR‐6 mutant with CRIB/PDZ domain in MDCK cells disturbs the cell‐cell contact‐induced junctional localization of tight junction proteins, as well as inhibiting TER development. Furthermore, the binding of Cdc42:GTP to the CRIB/PDZ domain of PAR‐6 enhances the kinase activity of PAR‐6‐bound aPKC. Detailed analyses suggest that the binding of PAR‐6 to aPKC has the intrinsic potential to activate aPKC, which is only released when Cdc42:GTP binds to the CRIB/PDZ domain . Conclusion The results indicate the involvement of PAR‐6 in the aPKC function which is required for the cell‐cell adhesion‐induced formation of epithelial junctional structures, possibly through the cooperative regulation of aPKC activity with Cdc42 .

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Metadata

Authors
Yamanaka, T., Horikoshi, Y., Suzuki, A., Sugiyama, Y., Kitamura, K., Maniwa, R., Nagai, Y., Yamashita, A., Hirose, T., Ishikawa, H., & Ohno, S.
Affiliations
Yokohama City University (JP)
Corresponding author
Ohno, Shigeo
ORCID
Venue
Genes to Cells
Publisher
Wiley
Published
2001-08
Volume
6
Issue
8
Pages
721-731
ISSN
  • 1356-9597 (ISSN-L)
  • 1365-2443
DOI
10.1046/j.1365-2443.2001.00453.x
OpenAlex
W1977245174
Cited by
306
References
47
Citations by year
2026: 2 · 2025: 5 · 2024: 4 · 2023: 2 · 2022: 7 · 2021: 7 · 2020: 13 · 2019: 8 · 2018: 9 · 2017: 13 · 2016: 8 · 2015: 11 · 2014: 19 · 2013: 16 · 2012: 16
FWCI
6.30
Type
journal article
Language
en
Open access
closed
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 141 d)
Locations
  • Genes to Cells (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Keywords
Par6, atypical protein kinase C, cell polarity, epithelial junctions, tight junctions, cell-cell contact, Cdc42, ternary complex, MDCK cells, transepithelial electrical resistance, cell adhesion
MeSH terms
Animals, Carrier Proteins, Cell Adhesion, Cell Communication, Cell Line, Cell Line, Transformed, Epithelial Cells, Guanosine Triphosphate, Humans, Intercellular Junctions, Mutation, Protein Binding, Protein Kinase C, Proteins, Transfection, Signal Transduction, Helminth Proteins, Cell Adhesion Molecules, Cell Polarity, Caenorhabditis elegans, Cell Cycle Proteins, COS Cells, cdc42 GTP-Binding Protein, Caenorhabditis elegans Proteins, Adaptor Proteins, Signal Transducing

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