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J. Biol. Chem., Vol. 276, Issue 46, 43205-43215, November 16, 2001
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From the Institute of Cancerology and Immunology of Marseille,
INSERM U.119, 27 bd Lei-Roure, 13009 Marseille, France
Nectins are adhesion molecules that
participate in the organization of epithelial and endothelial junctions
and serve as receptors for herpes simplex virus entry. They belong to
the immunoglobulin superfamily, are homologues of the poliovirus
receptor (PVR/CD155), and were also named poliovirus receptor-related
(PRR) proteins. We identify a new member of the nectin family named
nectin4. Peptide sequences of human and murine nectin4 share 92%
identity, and as for other members, the ectodomain is made of three
immunoglobulin-like domains of V, C, C types. In contrast to other
nectin molecules, detection of nectin4 transcripts is mainly restricted
to placenta in human tissues. Expression is broader in mouse, and
interestingly nectin4 is detected at days 11, 15, and 17 during murine
embryogenesis. Nectin4 interacts with afadin, a F-actin-associated
molecule, via its carboxyl-terminal cytoplasmic sequence. Both
molecules co-localize at cadherin-based adherens junctions in the
MDCKII epithelial cell line. Nectins are homophilic adhesion molecules, and recently heterophilic interactions have been described between nectin3/nectin1 and nectin3/nectin2. We confirmed these
trans-interactions and also described nectin3 as the PVR/CD155 ligand.
By means of several approaches, we report on the identification of
nectin4 as a new ligand for nectin1. First, a soluble chimeric
recombinant nectin4 ectodomain (nectin4-Fc) trans-interacts with cells
expressing nectin1 but not with cells expressing nectin2, nectin3, or
PVR/CD155. Conversely, nectin1-Fc binds to cells expressing nectin4.
Second, nectin1-Fc precipitates nectin4 expressed in COS cells.
Third, reciprocal in vitro physical interactions were
detected between nectin4-Fc and nectin1-Fc. The nectin4-Fc/nectin4-Fc
interaction was detected suggesting that nectin4 exhibits both
homophilic and heterophilic properties. Using the same approaches we
demonstrate, for the first time, that the V domain of nectin1 acts as a
major functional region involved in trans-heterointeraction with
nectin4 and also nectin3.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF426163 for human nectin4.
Nectin4/PRR4, a New Afadin-associated Member of the
Nectin Family That Trans-interacts with Nectin1/PRR1 through V Domain
Interaction*
*
This work was supported by INSERM, the Association pour la
Recherche Contre le Cancer (ARC), and the Ligue Nationale
Française Contre le Cancer (LNFCC).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
33-4-91-75-84-17; Fax: 33-4-91-26-03-64; E-mail:
lopez@marseille.inserm.fr.
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