J. Cell Biol., Volume 143, Number 1, October 5, 1998 95-106

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

Yasushi Izumi,^* Tomonori Hirose,^* Yoko Tamai,^* Syu-ichi Hirai,^* Yoji Nagashima, Toyoshi Fujimoto,^§ Yo Tabuse, Kenneth J. Kemphues,^¶ and Shigeo Ohno^*

^* Department of Molecular Biology and  Department of Pathology, Yokohama City University School of Medicine, Yokohama 236-0004, Japan; ^§ Department of Anatomy and Cell Biology, Gunma University School of Medicine, Maebashi 371-8511, Japan;  Fundamental Research Laboratories, NEC Corporation, Tsukuba 305-0841, Japan; and ^¶ Section of Genetics and Development, 101 Biotechnology Building, Cornell University, Ithaca, New York 14853

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 and PKC 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 PKC 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.

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