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J Biol Chem, Vol. 275, Issue 14, 10291-10299, April 7, 2000
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From the We have isolated a novel cell-cell adhesion
system localized at cadherin-based adherens junctions (AJs). This
system consists of at least nectin, a
Ca2+-independent immunoglobulin-like adhesion
molecule, and afadin, an actin filament-binding protein, that connects
nectin to the actin cytoskeleton. Nectin constitutes a family
consisting of two members, nectin-1 and -2. We have isolated here a
third member of the nectin family and named it nectin-3. Nectin-3 has
three splicing variants, nectin-3 Takai Biotimer Project, ERATO, Japan Science
and Technology Corporation, c/o JCR Pharmaceuticals Co., Ltd., 2-2-10 Murotani, Nishi-ku, Kobe 651-2241, Japan, the ¶ Department of
Molecular Biology and Biochemistry, Osaka University Graduate School of
Medicine/Faculty of Medicine, Suita 565-0871, Japan, and the
** Department of Anatomy and Neurobiology, Faculty of Medicine, Kyoto
University, Kyoto 606-8501, Japan
(biggest), -3
(middle), and
-3
(smallest). Like nectin-1 and -2, nectin-3 consists of three extracellular immunoglobulin-like domains, a transmembrane segment, and
a cytoplasmic region with the C-terminal consensus motif for binding to
the PDZ domain. Nectin-3 formed a cis-homo-dimer and showed Ca2+-independent trans-homo-interaction
to cause homophilic cell-cell adhesion. Nectin-3 furthermore showed
trans-hetero-interaction with nectin-1 or -2 but did not
form a cis-hetero-dimer with nectin-1 or -2. Nectin-1 did
not show trans-hetero-interaction with nectin-2. The
affinity of trans-hetero-interaction of nectin-3 with
nectin-1 or -2 was higher than that of
trans-homo-interaction of nectin-1, -2, or -3. Nectin-2
and -3 were ubiquitously expressed, whereas nectin-1 was abundantly
expressed in brain. Nectin-3 was colocalized with nectin-2 at
cadherin-based AJs and interacted with afadin. These results indicate
that the nectin family consists of at least three members, nectin-1,
-2, and -3, all of which show homophilic and heterophilic cell-cell
adhesion activities and are localized at cadherin-based AJs.
Present address: JCR Pharmaceuticals Co., Ltd., 2-2-10 Murotani, Nishi-ku, Kobe 651-2241, Japan.
To whom correspondence should be addressed: Dept. of Molecular
Biology and Biochemistry, Osaka University Graduate School of
Medicine/Faculty of Medicine, Suita 565-0871, Osaka, Japan. Tel.:
81-6-6879-3410; Fax: 81-6-6879-3419; E-mail:
ytakai@molbio.med.osaka-u.ac.jp.
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