title: Implications of nectin-like molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and transmembrane protein localization in epithelial cells.
abstract: Nectins are Ca2+-independent immunoglobulin-like cell-cell adhesion molecules that play roles in organization of a variety of cell-cell junctions in cooperation with or independently of cadherins. Four nectins have been identified. Five nectin-like molecules, which have domain structures similar to those of nectins, have been identified, and we characterized here nectin-like molecule-2 (Necl-2)/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1. Necl-2 showed Ca2+-independent homophilic cell-cell adhesion activity. It furthermore showed Ca2+-independent heterophilic cell-cell adhesion activity with Necl-1/TSLL1/SynCAM3 and nectin-3. Necl-2 was widely expressed in rat tissues examined. Necl-2 localized at the basolateral plasma membrane in epithelial cells of the mouse gall bladder, but not at specialized cell-cell junctions, such as tight junctions, adherens junctions, and desmosomes. Nectins bind afadin, whereas Necl-2 did not bind afadin but bound Pals2, a membrane-associated guanylate kinase family member known to bind Lin-7, implicated in the proper localization of the Let-23 protein in Caenorhabditis elegans, the homologue of mammalian epidermal growth factor receptor. These results indicate the unique localization of Necl-2 and its possible involvement in localization of a transmembrane protein(s) through Pals2.
authors.affiliation: Department of Molecular Biology and Biochemistry, Osaka University Graduate School of Medicine/Faculty of Medicine, Suita 565-0871, Osaka, Japan.
authors.forename: Tatsushi
authors.initials: T
authors.lastname: Shingai
authors.forename: Wataru
authors.initials: W
authors.lastname: Ikeda
authors.forename: Shigeki
authors.initials: S
authors.lastname: Kakunaga
authors.forename: Koji
authors.initials: K
authors.lastname: Morimoto
authors.forename: Kyoji
authors.initials: K
authors.lastname: Takekuni
authors.forename: Shinsuke
authors.initials: S
authors.lastname: Itoh
authors.forename: Keiko
authors.initials: K
authors.lastname: Satoh
authors.forename: Masakazu
authors.initials: M
authors.lastname: Takeuchi
authors.forename: Toshio
authors.initials: T
authors.lastname: Imai
authors.forename: Morito
authors.initials: M
authors.lastname: Monden
authors.forename: Yoshimi
authors.initials: Y
authors.lastname: Takai
mesh_terms: D000818:Animals; D002448:Cell Adhesion / Q000502:physiology*; D000075982:Cell Adhesion Molecule-1; D015815:Cell Adhesion Molecules / Q000235:genetics / Q000502:physiology*; D002462:Cell Membrane / Q000378:metabolism; D003001:Cloning, Molecular; D004847:Epithelial Cells / Q000502:physiology*; D005347:Fibroblasts / Q000502:physiology; D005822:Genetic Vectors; D007136:Immunoglobulins / Q000235:genetics / Q000502:physiology*; D007739:L Cells; D008565:Membrane Proteins / Q000235:genetics / Q000502:physiology*; D051379:Mice; D008969:Molecular Sequence Data; D009928:Organ Specificity; D010957:Plasmids; D011485:Protein Binding; D021381:Protein Transport; D051381:Rats; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000502:physiology; D014162:Transfection
chemical_list: C498598:Cadm1 protein, mouse; D000075982:Cell Adhesion Molecule-1; D015815:Cell Adhesion Molecules; D007136:Immunoglobulins; D008565:Membrane Proteins