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

doi:10.1083/jcb.143.1.95

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© The Rockefeller University Press, 0021-9525/1998//95 $5.00
The Journal of Cell Biology, Volume 143, Number 1, , 1998 95-106

Regular Articles

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 functionof most cells. Studies in mammalian epithelial cells have revealedthat the establishment and maintenance of cell polarity dependsupon cell adhesion, signaling networks, the cytoskeleton, andprotein transport. Atypical protein kinase C (PKC) isotypesPKC ${zeta}$ and PKC ${lambda}$ have been implicated in signaling through lipidmetabolites including phosphatidylinositol 3-phosphates, buttheir physiological role remains elusive. In the present studywe report the identification of a protein, ASIP (atypical PKCisotype–specific interacting protein), that binds to aPKCs, and show that it colocalizes with PKC ${lambda}$ to the cell junctionalcomplex in cultured epithelial MDCKII cells and rat intestinalepithelia. In addition, immunoelectron microscopy revealedthat ASIP localizes to tight junctions in intestinal epithelialcells. Furthermore, ASIP shows significant sequence similarityto Caenorhabditis elegans PAR-3. PAR-3 protein is localizedto the anterior periphery of the one-cell embryo, and is required for the establishment of cell polarity in early embryos. ASIPand PAR-3 share three PDZ domains, and can both bind to aPKCs.Taken together, our results suggest a role for a protein complexcontaining ASIP and aPKC in the establishment and/or maintenanceof epithelial cell polarity. The evolutionary conservation of the protein complex and its asymmetric distribution in polarizedcells from worm embryo to mammalian-differentiated cells maymean that the complex functions generally in the organizationof cellular asymmetry.

Key Words: ASIP • atypical PKC • par • cell polarity • tight junction

Abbreviations used in this paper: ASIP, atypical PKC isotype–specific interacting protein; GST, glutathione-S-transferase; PKC, protein kinase C; PVDF, polyvinylidene difluoride; tag-ASIP, epitope-tagged-ASIP.

Address all correspondence to Dr. Shigeo Ohno, Department ofMolecular Biology, Yokohama City University School of Medicine,Kanazawa-ku, Yokohama 236-0004, Japan. Tel.: 81-45-787-2596.Fax: 81-45-785-4140. E-mail: ohnos{at}med.yokohama-cu.ac.jp

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