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Yoshimi Takai - One of the best experts on this subject based on the ideXlab platform.

  • nectin like molecule 1 tsll1 syncam3 a neural tissue specific immunoglobulin like Cell Cell adhesion molecule localizing at non junctional contact sites of presynaptic nerve terminals axons and Glia Cell processes
    Journal of Cell Science, 2005
    Co-Authors: Shigeki Kakunaga, Wataru Ikeda, Shinsuke Itoh, Toshihisa Ohtsuka, Akira Mizoguchi, Maki Deguchitawarada, Yoshimi Takai
    Abstract:

    Nectins are Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecules and comprise a family of four members. At the mossy fiber terminals of hippocampus, nectin-1 and nectin-3 localize at the presynaptic and postsynaptic sides of synaptic junctions, respectively, and their trans-interactions play a role in formation of synapses in cooperation with N-cadherin. Nectins are associated with the actin cytoskeleton through afadin, a nectin- and actin-filament-binding protein. Five nectin-like molecules (Necls) which have domain structures similar to those of nectins have been identified and here we characterize Necl-1/TSLL1/SynCAM3, from now on referred to as Necl-1. Tissue distribution analysis showed that Necl-1 was specifically expressed in the neural tissue. Immunofluorescence and immunoelectron microscopy revealed that Necl-1 localized at the contact sites among axons, their terminals, and Glia Cell processes that cooperatively formed synapses, axon bundles and myelinated axons. Necl-1 showed Ca2+-independent homophilic Cell-Cell adhesion activity. It furthermore showed Ca2+-independent heterophilic Cell-Cell adhesion activity with Necl-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 from now on referred to as Necl-2, nectin-1 and nectin-3, but not with Necl-5 or nectin-2. The C-terminal cytoplasmic region of Necl-1 did not bind afadin but bound membrane-associated guanylate kinase subfamily members that contain the L27 domain, including Dlg3, Pals2 and CASK. These results indicate that Necl-1 is a neural-tissue-specific Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecule which potentially has membrane-associated guanylate kinase subfamily member-binding activity and localizes at the non-junctional Cell-Cell contact sites.

  • Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific immunoglobulin-like Cell-Cell adhesion molecule localizing at non-junctional contact sites of presynaptic nerve terminals, axons and Glia Cell processes
    Journal of Cell Science, 2005
    Co-Authors: Shigeki Kakunaga, Wataru Ikeda, Shinsuke Itoh, Maki Deguchi-tawarada, Toshihisa Ohtsuka, Akira Mizoguchi, Yoshimi Takai
    Abstract:

    Nectins are Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecules and comprise a family of four members. At the mossy fiber terminals of hippocampus, nectin-1 and nectin-3 localize at the presynaptic and postsynaptic sides of synaptic junctions, respectively, and their trans-interactions play a role in formation of synapses in cooperation with N-cadherin. Nectins are associated with the actin cytoskeleton through afadin, a nectin- and actin-filament-binding protein. Five nectin-like molecules (Necls) which have domain structures similar to those of nectins have been identified and here we characterize Necl-1/TSLL1/SynCAM3, from now on referred to as Necl-1. Tissue distribution analysis showed that Necl-1 was specifically expressed in the neural tissue. Immunofluorescence and immunoelectron microscopy revealed that Necl-1 localized at the contact sites among axons, their terminals, and Glia Cell processes that cooperatively formed synapses, axon bundles and myelinated axons. Necl-1 showed Ca2+-independent homophilic Cell-Cell adhesion activity. It furthermore showed Ca2+-independent heterophilic Cell-Cell adhesion activity with Necl-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 from now on referred to as Necl-2, nectin-1 and nectin-3, but not with Necl-5 or nectin-2. The C-terminal cytoplasmic region of Necl-1 did not bind afadin but bound membrane-associated guanylate kinase subfamily members that contain the L27 domain, including Dlg3, Pals2 and CASK. These results indicate that Necl-1 is a neural-tissue-specific Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecule which potentially has membrane-associated guanylate kinase subfamily member-binding activity and localizes at the non-junctional Cell-Cell contact sites.

Shigeki Kakunaga - One of the best experts on this subject based on the ideXlab platform.

  • nectin like molecule 1 tsll1 syncam3 a neural tissue specific immunoglobulin like Cell Cell adhesion molecule localizing at non junctional contact sites of presynaptic nerve terminals axons and Glia Cell processes
    Journal of Cell Science, 2005
    Co-Authors: Shigeki Kakunaga, Wataru Ikeda, Shinsuke Itoh, Toshihisa Ohtsuka, Akira Mizoguchi, Maki Deguchitawarada, Yoshimi Takai
    Abstract:

    Nectins are Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecules and comprise a family of four members. At the mossy fiber terminals of hippocampus, nectin-1 and nectin-3 localize at the presynaptic and postsynaptic sides of synaptic junctions, respectively, and their trans-interactions play a role in formation of synapses in cooperation with N-cadherin. Nectins are associated with the actin cytoskeleton through afadin, a nectin- and actin-filament-binding protein. Five nectin-like molecules (Necls) which have domain structures similar to those of nectins have been identified and here we characterize Necl-1/TSLL1/SynCAM3, from now on referred to as Necl-1. Tissue distribution analysis showed that Necl-1 was specifically expressed in the neural tissue. Immunofluorescence and immunoelectron microscopy revealed that Necl-1 localized at the contact sites among axons, their terminals, and Glia Cell processes that cooperatively formed synapses, axon bundles and myelinated axons. Necl-1 showed Ca2+-independent homophilic Cell-Cell adhesion activity. It furthermore showed Ca2+-independent heterophilic Cell-Cell adhesion activity with Necl-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 from now on referred to as Necl-2, nectin-1 and nectin-3, but not with Necl-5 or nectin-2. The C-terminal cytoplasmic region of Necl-1 did not bind afadin but bound membrane-associated guanylate kinase subfamily members that contain the L27 domain, including Dlg3, Pals2 and CASK. These results indicate that Necl-1 is a neural-tissue-specific Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecule which potentially has membrane-associated guanylate kinase subfamily member-binding activity and localizes at the non-junctional Cell-Cell contact sites.

  • Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific immunoglobulin-like Cell-Cell adhesion molecule localizing at non-junctional contact sites of presynaptic nerve terminals, axons and Glia Cell processes
    Journal of Cell Science, 2005
    Co-Authors: Shigeki Kakunaga, Wataru Ikeda, Shinsuke Itoh, Maki Deguchi-tawarada, Toshihisa Ohtsuka, Akira Mizoguchi, Yoshimi Takai
    Abstract:

    Nectins are Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecules and comprise a family of four members. At the mossy fiber terminals of hippocampus, nectin-1 and nectin-3 localize at the presynaptic and postsynaptic sides of synaptic junctions, respectively, and their trans-interactions play a role in formation of synapses in cooperation with N-cadherin. Nectins are associated with the actin cytoskeleton through afadin, a nectin- and actin-filament-binding protein. Five nectin-like molecules (Necls) which have domain structures similar to those of nectins have been identified and here we characterize Necl-1/TSLL1/SynCAM3, from now on referred to as Necl-1. Tissue distribution analysis showed that Necl-1 was specifically expressed in the neural tissue. Immunofluorescence and immunoelectron microscopy revealed that Necl-1 localized at the contact sites among axons, their terminals, and Glia Cell processes that cooperatively formed synapses, axon bundles and myelinated axons. Necl-1 showed Ca2+-independent homophilic Cell-Cell adhesion activity. It furthermore showed Ca2+-independent heterophilic Cell-Cell adhesion activity with Necl-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 from now on referred to as Necl-2, nectin-1 and nectin-3, but not with Necl-5 or nectin-2. The C-terminal cytoplasmic region of Necl-1 did not bind afadin but bound membrane-associated guanylate kinase subfamily members that contain the L27 domain, including Dlg3, Pals2 and CASK. These results indicate that Necl-1 is a neural-tissue-specific Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecule which potentially has membrane-associated guanylate kinase subfamily member-binding activity and localizes at the non-junctional Cell-Cell contact sites.

Toshihisa Ohtsuka - One of the best experts on this subject based on the ideXlab platform.

  • nectin like molecule 1 tsll1 syncam3 a neural tissue specific immunoglobulin like Cell Cell adhesion molecule localizing at non junctional contact sites of presynaptic nerve terminals axons and Glia Cell processes
    Journal of Cell Science, 2005
    Co-Authors: Shigeki Kakunaga, Wataru Ikeda, Shinsuke Itoh, Toshihisa Ohtsuka, Akira Mizoguchi, Maki Deguchitawarada, Yoshimi Takai
    Abstract:

    Nectins are Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecules and comprise a family of four members. At the mossy fiber terminals of hippocampus, nectin-1 and nectin-3 localize at the presynaptic and postsynaptic sides of synaptic junctions, respectively, and their trans-interactions play a role in formation of synapses in cooperation with N-cadherin. Nectins are associated with the actin cytoskeleton through afadin, a nectin- and actin-filament-binding protein. Five nectin-like molecules (Necls) which have domain structures similar to those of nectins have been identified and here we characterize Necl-1/TSLL1/SynCAM3, from now on referred to as Necl-1. Tissue distribution analysis showed that Necl-1 was specifically expressed in the neural tissue. Immunofluorescence and immunoelectron microscopy revealed that Necl-1 localized at the contact sites among axons, their terminals, and Glia Cell processes that cooperatively formed synapses, axon bundles and myelinated axons. Necl-1 showed Ca2+-independent homophilic Cell-Cell adhesion activity. It furthermore showed Ca2+-independent heterophilic Cell-Cell adhesion activity with Necl-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 from now on referred to as Necl-2, nectin-1 and nectin-3, but not with Necl-5 or nectin-2. The C-terminal cytoplasmic region of Necl-1 did not bind afadin but bound membrane-associated guanylate kinase subfamily members that contain the L27 domain, including Dlg3, Pals2 and CASK. These results indicate that Necl-1 is a neural-tissue-specific Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecule which potentially has membrane-associated guanylate kinase subfamily member-binding activity and localizes at the non-junctional Cell-Cell contact sites.

  • Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific immunoglobulin-like Cell-Cell adhesion molecule localizing at non-junctional contact sites of presynaptic nerve terminals, axons and Glia Cell processes
    Journal of Cell Science, 2005
    Co-Authors: Shigeki Kakunaga, Wataru Ikeda, Shinsuke Itoh, Maki Deguchi-tawarada, Toshihisa Ohtsuka, Akira Mizoguchi, Yoshimi Takai
    Abstract:

    Nectins are Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecules and comprise a family of four members. At the mossy fiber terminals of hippocampus, nectin-1 and nectin-3 localize at the presynaptic and postsynaptic sides of synaptic junctions, respectively, and their trans-interactions play a role in formation of synapses in cooperation with N-cadherin. Nectins are associated with the actin cytoskeleton through afadin, a nectin- and actin-filament-binding protein. Five nectin-like molecules (Necls) which have domain structures similar to those of nectins have been identified and here we characterize Necl-1/TSLL1/SynCAM3, from now on referred to as Necl-1. Tissue distribution analysis showed that Necl-1 was specifically expressed in the neural tissue. Immunofluorescence and immunoelectron microscopy revealed that Necl-1 localized at the contact sites among axons, their terminals, and Glia Cell processes that cooperatively formed synapses, axon bundles and myelinated axons. Necl-1 showed Ca2+-independent homophilic Cell-Cell adhesion activity. It furthermore showed Ca2+-independent heterophilic Cell-Cell adhesion activity with Necl-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 from now on referred to as Necl-2, nectin-1 and nectin-3, but not with Necl-5 or nectin-2. The C-terminal cytoplasmic region of Necl-1 did not bind afadin but bound membrane-associated guanylate kinase subfamily members that contain the L27 domain, including Dlg3, Pals2 and CASK. These results indicate that Necl-1 is a neural-tissue-specific Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecule which potentially has membrane-associated guanylate kinase subfamily member-binding activity and localizes at the non-junctional Cell-Cell contact sites.

Shinsuke Itoh - One of the best experts on this subject based on the ideXlab platform.

  • nectin like molecule 1 tsll1 syncam3 a neural tissue specific immunoglobulin like Cell Cell adhesion molecule localizing at non junctional contact sites of presynaptic nerve terminals axons and Glia Cell processes
    Journal of Cell Science, 2005
    Co-Authors: Shigeki Kakunaga, Wataru Ikeda, Shinsuke Itoh, Toshihisa Ohtsuka, Akira Mizoguchi, Maki Deguchitawarada, Yoshimi Takai
    Abstract:

    Nectins are Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecules and comprise a family of four members. At the mossy fiber terminals of hippocampus, nectin-1 and nectin-3 localize at the presynaptic and postsynaptic sides of synaptic junctions, respectively, and their trans-interactions play a role in formation of synapses in cooperation with N-cadherin. Nectins are associated with the actin cytoskeleton through afadin, a nectin- and actin-filament-binding protein. Five nectin-like molecules (Necls) which have domain structures similar to those of nectins have been identified and here we characterize Necl-1/TSLL1/SynCAM3, from now on referred to as Necl-1. Tissue distribution analysis showed that Necl-1 was specifically expressed in the neural tissue. Immunofluorescence and immunoelectron microscopy revealed that Necl-1 localized at the contact sites among axons, their terminals, and Glia Cell processes that cooperatively formed synapses, axon bundles and myelinated axons. Necl-1 showed Ca2+-independent homophilic Cell-Cell adhesion activity. It furthermore showed Ca2+-independent heterophilic Cell-Cell adhesion activity with Necl-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 from now on referred to as Necl-2, nectin-1 and nectin-3, but not with Necl-5 or nectin-2. The C-terminal cytoplasmic region of Necl-1 did not bind afadin but bound membrane-associated guanylate kinase subfamily members that contain the L27 domain, including Dlg3, Pals2 and CASK. These results indicate that Necl-1 is a neural-tissue-specific Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecule which potentially has membrane-associated guanylate kinase subfamily member-binding activity and localizes at the non-junctional Cell-Cell contact sites.

  • Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific immunoglobulin-like Cell-Cell adhesion molecule localizing at non-junctional contact sites of presynaptic nerve terminals, axons and Glia Cell processes
    Journal of Cell Science, 2005
    Co-Authors: Shigeki Kakunaga, Wataru Ikeda, Shinsuke Itoh, Maki Deguchi-tawarada, Toshihisa Ohtsuka, Akira Mizoguchi, Yoshimi Takai
    Abstract:

    Nectins are Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecules and comprise a family of four members. At the mossy fiber terminals of hippocampus, nectin-1 and nectin-3 localize at the presynaptic and postsynaptic sides of synaptic junctions, respectively, and their trans-interactions play a role in formation of synapses in cooperation with N-cadherin. Nectins are associated with the actin cytoskeleton through afadin, a nectin- and actin-filament-binding protein. Five nectin-like molecules (Necls) which have domain structures similar to those of nectins have been identified and here we characterize Necl-1/TSLL1/SynCAM3, from now on referred to as Necl-1. Tissue distribution analysis showed that Necl-1 was specifically expressed in the neural tissue. Immunofluorescence and immunoelectron microscopy revealed that Necl-1 localized at the contact sites among axons, their terminals, and Glia Cell processes that cooperatively formed synapses, axon bundles and myelinated axons. Necl-1 showed Ca2+-independent homophilic Cell-Cell adhesion activity. It furthermore showed Ca2+-independent heterophilic Cell-Cell adhesion activity with Necl-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 from now on referred to as Necl-2, nectin-1 and nectin-3, but not with Necl-5 or nectin-2. The C-terminal cytoplasmic region of Necl-1 did not bind afadin but bound membrane-associated guanylate kinase subfamily members that contain the L27 domain, including Dlg3, Pals2 and CASK. These results indicate that Necl-1 is a neural-tissue-specific Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecule which potentially has membrane-associated guanylate kinase subfamily member-binding activity and localizes at the non-junctional Cell-Cell contact sites.

Wataru Ikeda - One of the best experts on this subject based on the ideXlab platform.

  • nectin like molecule 1 tsll1 syncam3 a neural tissue specific immunoglobulin like Cell Cell adhesion molecule localizing at non junctional contact sites of presynaptic nerve terminals axons and Glia Cell processes
    Journal of Cell Science, 2005
    Co-Authors: Shigeki Kakunaga, Wataru Ikeda, Shinsuke Itoh, Toshihisa Ohtsuka, Akira Mizoguchi, Maki Deguchitawarada, Yoshimi Takai
    Abstract:

    Nectins are Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecules and comprise a family of four members. At the mossy fiber terminals of hippocampus, nectin-1 and nectin-3 localize at the presynaptic and postsynaptic sides of synaptic junctions, respectively, and their trans-interactions play a role in formation of synapses in cooperation with N-cadherin. Nectins are associated with the actin cytoskeleton through afadin, a nectin- and actin-filament-binding protein. Five nectin-like molecules (Necls) which have domain structures similar to those of nectins have been identified and here we characterize Necl-1/TSLL1/SynCAM3, from now on referred to as Necl-1. Tissue distribution analysis showed that Necl-1 was specifically expressed in the neural tissue. Immunofluorescence and immunoelectron microscopy revealed that Necl-1 localized at the contact sites among axons, their terminals, and Glia Cell processes that cooperatively formed synapses, axon bundles and myelinated axons. Necl-1 showed Ca2+-independent homophilic Cell-Cell adhesion activity. It furthermore showed Ca2+-independent heterophilic Cell-Cell adhesion activity with Necl-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 from now on referred to as Necl-2, nectin-1 and nectin-3, but not with Necl-5 or nectin-2. The C-terminal cytoplasmic region of Necl-1 did not bind afadin but bound membrane-associated guanylate kinase subfamily members that contain the L27 domain, including Dlg3, Pals2 and CASK. These results indicate that Necl-1 is a neural-tissue-specific Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecule which potentially has membrane-associated guanylate kinase subfamily member-binding activity and localizes at the non-junctional Cell-Cell contact sites.

  • Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific immunoglobulin-like Cell-Cell adhesion molecule localizing at non-junctional contact sites of presynaptic nerve terminals, axons and Glia Cell processes
    Journal of Cell Science, 2005
    Co-Authors: Shigeki Kakunaga, Wataru Ikeda, Shinsuke Itoh, Maki Deguchi-tawarada, Toshihisa Ohtsuka, Akira Mizoguchi, Yoshimi Takai
    Abstract:

    Nectins are Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecules and comprise a family of four members. At the mossy fiber terminals of hippocampus, nectin-1 and nectin-3 localize at the presynaptic and postsynaptic sides of synaptic junctions, respectively, and their trans-interactions play a role in formation of synapses in cooperation with N-cadherin. Nectins are associated with the actin cytoskeleton through afadin, a nectin- and actin-filament-binding protein. Five nectin-like molecules (Necls) which have domain structures similar to those of nectins have been identified and here we characterize Necl-1/TSLL1/SynCAM3, from now on referred to as Necl-1. Tissue distribution analysis showed that Necl-1 was specifically expressed in the neural tissue. Immunofluorescence and immunoelectron microscopy revealed that Necl-1 localized at the contact sites among axons, their terminals, and Glia Cell processes that cooperatively formed synapses, axon bundles and myelinated axons. Necl-1 showed Ca2+-independent homophilic Cell-Cell adhesion activity. It furthermore showed Ca2+-independent heterophilic Cell-Cell adhesion activity with Necl-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 from now on referred to as Necl-2, nectin-1 and nectin-3, but not with Necl-5 or nectin-2. The C-terminal cytoplasmic region of Necl-1 did not bind afadin but bound membrane-associated guanylate kinase subfamily members that contain the L27 domain, including Dlg3, Pals2 and CASK. These results indicate that Necl-1 is a neural-tissue-specific Ca2+-independent immunoglobulin-like Cell-Cell adhesion molecule which potentially has membrane-associated guanylate kinase subfamily member-binding activity and localizes at the non-junctional Cell-Cell contact sites.