Involvement of the interaction of afadin with ZO-1 in the formation of tight junctions in Madin-Darby canine kidney cells. 2010

Takako Ooshio, and Reiko Kobayashi, and Wataru Ikeda, and Muneaki Miyata, and Yuri Fukumoto, and Naomi Matsuzawa, and Hisakazu Ogita, and Yoshimi Takai
Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine, Suita, Osaka 565-0871, Japan.

Tight junctions (TJs) and adherens junctions (AJs) are major junctional apparatuses in epithelial cells. Claudins and junctional adhesion molecules (JAMs) are major cell adhesion molecules (CAMs) at TJs, whereas cadherins and nectins are major CAMs at AJs. Claudins and JAMs are associated with ZO proteins, whereas cadherins are associated with beta- and alpha-catenins, and nectins are associated with afadin. We previously showed that nectins first form cell-cell adhesions where the cadherin-catenin complex is recruited to form AJs, followed by the recruitment of the JAM-ZO and claudin-ZO complexes to the apical side of AJs to form TJs. It is not fully understood how TJ components are recruited to the apical side of AJs. We studied the roles of afadin and ZO-1 in the formation of TJs in Madin-Darby canine kidney (MDCK) cells. Before the formation of TJs, ZO-1 interacted with afadin through the two proline-rich regions of afadin and the SH3 domain of ZO-1. During and after the formation of TJs, ZO-1 dissociated from afadin and associated with JAM-A. Knockdown of afadin impaired the formation of both AJs and TJs in MDCK cells, whereas knockdown of ZO-1 impaired the formation of TJs, but not AJs. Re-expression of full-length afadin restored the formation of both AJs and TJs in afadin-knockdown MDCK cells, whereas re-expression of afadin-DeltaPR1-2, which is incapable of binding to ZO-1, restored the formation of AJs, but not TJs. These results indicate that the transient interaction of afadin with ZO-1 is necessary for the formation of TJs in MDCK cells.

UI MeSH Term Description Entries
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D008840 Microfilament Proteins Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell. Actin Binding Protein,Actin-Binding Protein,Actin-Binding Proteins,Microfilament Protein,Actin Binding Proteins,Binding Protein, Actin,Protein, Actin Binding,Protein, Actin-Binding,Protein, Microfilament,Proteins, Actin-Binding,Proteins, Microfilament
D008856 Microscopy, Fluorescence Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye. Fluorescence Microscopy,Immunofluorescence Microscopy,Microscopy, Immunofluorescence,Fluorescence Microscopies,Immunofluorescence Microscopies,Microscopies, Fluorescence,Microscopies, Immunofluorescence
D010750 Phosphoproteins Phosphoprotein
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D002118 Calcium A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D004285 Dogs The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065) Canis familiaris,Dog
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D019108 Tight Junctions Cell-cell junctions that seal adjacent epithelial cells together, preventing the passage of most dissolved molecules from one side of the epithelial sheet to the other. (Alberts et al., Molecular Biology of the Cell, 2nd ed, p22) Occluding Junctions,Zonula Occludens,Junction, Occluding,Junction, Tight,Junctions, Occluding,Junctions, Tight,Occluden, Zonula,Occludens, Zonula,Occluding Junction,Tight Junction,Zonula Occluden

Related Publications

Takako Ooshio, and Reiko Kobayashi, and Wataru Ikeda, and Muneaki Miyata, and Yuri Fukumoto, and Naomi Matsuzawa, and Hisakazu Ogita, and Yoshimi Takai
April 2006, Molecular biology of the cell,
Takako Ooshio, and Reiko Kobayashi, and Wataru Ikeda, and Muneaki Miyata, and Yuri Fukumoto, and Naomi Matsuzawa, and Hisakazu Ogita, and Yoshimi Takai
April 1988, The Journal of cell biology,
Takako Ooshio, and Reiko Kobayashi, and Wataru Ikeda, and Muneaki Miyata, and Yuri Fukumoto, and Naomi Matsuzawa, and Hisakazu Ogita, and Yoshimi Takai
October 1989, The Biochemical journal,
Takako Ooshio, and Reiko Kobayashi, and Wataru Ikeda, and Muneaki Miyata, and Yuri Fukumoto, and Naomi Matsuzawa, and Hisakazu Ogita, and Yoshimi Takai
December 2003, The Journal of biological chemistry,
Takako Ooshio, and Reiko Kobayashi, and Wataru Ikeda, and Muneaki Miyata, and Yuri Fukumoto, and Naomi Matsuzawa, and Hisakazu Ogita, and Yoshimi Takai
August 2001, Molecular biology of the cell,
Takako Ooshio, and Reiko Kobayashi, and Wataru Ikeda, and Muneaki Miyata, and Yuri Fukumoto, and Naomi Matsuzawa, and Hisakazu Ogita, and Yoshimi Takai
December 1988, The Journal of cell biology,
Takako Ooshio, and Reiko Kobayashi, and Wataru Ikeda, and Muneaki Miyata, and Yuri Fukumoto, and Naomi Matsuzawa, and Hisakazu Ogita, and Yoshimi Takai
February 2006, The Journal of biological chemistry,
Takako Ooshio, and Reiko Kobayashi, and Wataru Ikeda, and Muneaki Miyata, and Yuri Fukumoto, and Naomi Matsuzawa, and Hisakazu Ogita, and Yoshimi Takai
December 1988, The Journal of cell biology,
Takako Ooshio, and Reiko Kobayashi, and Wataru Ikeda, and Muneaki Miyata, and Yuri Fukumoto, and Naomi Matsuzawa, and Hisakazu Ogita, and Yoshimi Takai
February 2005, The Journal of biological chemistry,
Takako Ooshio, and Reiko Kobayashi, and Wataru Ikeda, and Muneaki Miyata, and Yuri Fukumoto, and Naomi Matsuzawa, and Hisakazu Ogita, and Yoshimi Takai
October 2004, TheScientificWorldJournal,
Copied contents to your clipboard!