DOI: 10.1083/jcb.143.1.95. An Atypical PKC Directly Associates and Colocalizes at the Epithelial Tight Junction with ASIP, a Mammalian Homologue of <i>Caenorhabditis elegans</i> Polarity Protein PAR-3

An Atypical PKC Directly Associates and Colocalizes at the Epithelial Tight Junction with ASIP, a Mammalian Homologue of Caenorhabditis elegans Polarity Protein PAR-3

10.1083/jcb.143.1.95

Crossref journal-article

Rockefeller University Press

The Journal of Cell Biology (291)

Abstract

Cell polarity is fundamental to differentiation and function of most cells. Studies in mammalian epithelial cells have revealed that the establishment and maintenance of cell polarity depends upon cell adhesion, signaling networks, the cytoskeleton, and protein transport. Atypical protein kinase C (PKC) isotypes PKCζ and PKCλ have been implicated in signaling through lipid metabolites including phosphatidylinositol 3-phosphates, but their physiological role remains elusive. In the present study we report the identification of a protein, ASIP (atypical PKC isotype–specific interacting protein), that binds to aPKCs, and show that it colocalizes with PKCλ to the cell junctional complex in cultured epithelial MDCKII cells and rat intestinal epithelia. In addition, immunoelectron microscopy revealed that ASIP localizes to tight junctions in intestinal epithelial cells. Furthermore, ASIP shows significant sequence similarity to Caenorhabditis elegans PAR-3. PAR-3 protein is localized to the anterior periphery of the one-cell embryo, and is required for the establishment of cell polarity in early embryos. ASIP and PAR-3 share three PDZ domains, and can both bind to aPKCs. Taken together, our results suggest a role for a protein complex containing ASIP and aPKC in the establishment and/or maintenance of epithelial cell polarity. The evolutionary conservation of the protein complex and its asymmetric distribution in polarized cells from worm embryo to mammalian-differentiated cells may mean that the complex functions generally in the organization of cellular asymmetry.

Bibliography

Izumi, Y., Hirose, T., Tamai, Y., Hirai, S., Nagashima, Y., Fujimoto, T., Tabuse, Y., Kemphues, K. J., & Ohno, S. (1998). An Atypical PKC Directly Associates and Colocalizes at the Epithelial Tight Junction with ASIP, a Mammalian Homologue of Caenorhabditis elegans Polarity Protein PAR-3. The Journal of Cell Biology, 143(1), 95â106.

Authors 9

Yasushi Izumi (first)
Tomonori Hirose (additional)
Yoko Tamai (additional)
Syu-ichi Hirai (additional)
Yoji Nagashima (additional)
Toyoshi Fujimoto (additional)
Yo Tabuse (additional)
Kenneth J. Kemphues (additional)
Shigeo Ohno (additional)

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Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 12:47 p.m.)
Deposited	2 years, 1 month ago (July 28, 2023, 8:22 p.m.)
Indexed	1 month, 2 weeks ago (July 14, 2025, 11:30 p.m.)
Issued	26 years, 10 months ago (Oct. 5, 1998)
Published	26 years, 10 months ago (Oct. 5, 1998)
Published Online	26 years, 10 months ago (Oct. 5, 1998)
Published Print	26 years, 10 months ago (Oct. 5, 1998)

Funders 0

None

BibTeX

@article{Izumi_1998, title={An Atypical PKC Directly Associates and Colocalizes at the Epithelial Tight Junction with ASIP, a Mammalian Homologue of Caenorhabditis elegans Polarity Protein PAR-3}, volume={143}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.143.1.95}, DOI={10.1083/jcb.143.1.95}, number={1}, journal={The Journal of Cell Biology}, publisher={Rockefeller University Press}, author={Izumi, Yasushi and Hirose, Tomonori and Tamai, Yoko and Hirai, Syu-ichi and Nagashima, Yoji and Fujimoto, Toyoshi and Tabuse, Yo and Kemphues, Kenneth J. and Ohno, Shigeo}, year={1998}, month=oct, pages={95–106} }

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  "abstract": "<jats:p>Cell polarity is fundamental to differentiation and function of most cells. Studies in mammalian epithelial cells have revealed that the establishment and maintenance of cell polarity depends upon cell adhesion, signaling networks, the cytoskeleton, and protein transport. Atypical protein kinase C (PKC) isotypes PKC\u03b6 and PKC\u03bb have been implicated in signaling through lipid metabolites including phosphatidylinositol 3-phosphates, but their physiological role remains elusive. In the present study we report the identification of a protein, ASIP (atypical PKC isotype\u2013specific interacting protein), that binds to aPKCs, and show that it colocalizes with PKC\u03bb to the cell junctional complex in cultured epithelial MDCKII cells and rat intestinal epithelia. In addition, immunoelectron microscopy revealed that ASIP localizes to tight junctions in intestinal epithelial cells. Furthermore, ASIP shows significant sequence similarity to Caenorhabditis elegans PAR-3. PAR-3 protein is localized to the anterior periphery of the one-cell embryo, and is required for the establishment of cell polarity in early embryos. ASIP and PAR-3 share three PDZ domains, and can both bind to aPKCs. Taken together, our results suggest a role for a protein complex containing ASIP and aPKC in the establishment and/or maintenance of epithelial cell polarity. The evolutionary conservation of the protein complex and its asymmetric distribution in polarized cells from worm embryo to mammalian-differentiated cells may mean that the complex functions generally in the organization of cellular asymmetry.</jats:p>",
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