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First published online July 2, 2007
doi: 10.1242/10.1242/jcs.03470

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Cooperative roles of Par-3 and afadin in the formation of adherens and tight junctions

Takako Ooshio¹, Naoyuki Fujita¹, Akio Yamada¹, Tatsuhiro Sato¹, Yuichi Kitagawa¹, Ryoko Okamoto¹, Shinsuke Nakata¹, Ayaka Miki¹, Kenji Irie^1,* and Yoshimi Takai^1,2,

¹ Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Osaka, Japan
² Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine/Faculty of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe 650-0017, Hyogo, Japan

Author for correspondence (e-mail: ytakai{at}molbio.med.osaka-u.ac.jp)

Accepted 14 May 2007

Par-3 is a cell-polarity protein that regulates the formation of tight junctions (TJs) in epithelial cells, where claudin is a major cell-cell adhesion molecule (CAM). TJs are formed at the apical side of adherens junctions (AJs), where E-cadherin and nectin are major CAMs. We have revealed that nectin first forms cell-cell adhesions, and then recruits cadherin to nectin-based cell-cell adhesion sites to form AJs and subsequently recruits claudin to the apical side of AJs to form TJs. The cytoplasmic tail of nectin binds afadin and Par-3. Afadin regulates the formation of AJs and TJs cooperatively with nectin. Here, we studied the role of Par-3 in the formation of these junctions by using Par-3-knockdown MDCK cells. Par-3 was necessary for the formation of AJs and TJs but was not necessary for nectin-based cell-cell adhesion. Par-3 promoted the association of afadin with nectin, whereas afadin was not necessary for the association of Par-3 with nectin. However, the association of afadin with nectin alone was not sufficient for the formation of AJs or TJs, and Par-3 and afadin cooperatively regulated it. We describe here these novel roles of Par-3 in the formation of junctional complexes.

Key words: Adherens junctions, Tight junctions, Nectin, Par-3, Afadin

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