Fibronectin Type III-like Domains of Neurofascin-186 Protein Mediate Gliomedin Binding and Its Clustering at the Developing Nodes of Ranvier*
| Autor: | Catherine Faivre-Sarrailh, Jérôme Devaux, Christian Lévêque, Marilyne Labasque |
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| Přispěvatelé: | Centre de recherche en neurobiologie - neurophysiologie de Marseille (CRN2M), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
MESH: Myelin Sheath
Immunoglobulin domain Biochemistry Myelin MESH: Protein Structure Tertiary 0302 clinical medicine Neurobiology MESH: Fibronectins Neural Cell Adhesion Molecules Myelin Sheath 0303 health sciences Node of Ranvier Cell adhesion molecule Cell biology MESH: Surface Plasmon Resonance medicine.anatomical_structure MESH: HEK293 Cells MESH: Cell Adhesion Molecules MESH: Neuroglia Neuroglia Protein Binding MESH: Axons MESH: Cell Line Tumor Schwann cell Nerve Tissue Proteins Biology MESH: Cell Adhesion Cell Line 03 medical and health sciences Cell Line Tumor Ranvier's Nodes medicine Cell Adhesion MESH: Protein Binding Humans Nerve Growth Factors [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] Cell adhesion Molecular Biology 030304 developmental biology MESH: Humans MESH: Nerve Growth Factors Membrane Proteins Cell Biology Surface Plasmon Resonance Axons MESH: Cell Line Fibronectins Protein Structure Tertiary HEK293 Cells nervous system MESH: Neural Cell Adhesion Molecules Immunoglobulin superfamily Neural cell adhesion molecule MESH: Ranvier's Nodes Schwann Cells MESH: Schwann Cells Cell Adhesion Molecules 030217 neurology & neurosurgery |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2011, 286 (49), pp.42426-34. ⟨10.1074/jbc.M111.266353⟩ Journal of Biological Chemistry, 2011, 286 (49), pp.42426-34. ⟨10.1074/jbc.M111.266353⟩ |
| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.M111.266353⟩ |
| Popis: | International audience; The cell adhesion molecules (CAMs) of the immunoglobulin superfamily (Ig-CAMs) play a crucial role in the organization of the node of Ranvier in myelinated axons. In the peripheral nervous system, Gliomedin (Gldn) secreted by Schwann cell microvilli binds NgCAM-related CAM (NrCAM) and Neurofascin-186 (NF186) and direct the nodal clustering of voltage-gated sodium channels (Nav). NF186 is the single axonal Gldn partner to ensure Nav clustering at nodes, whereas NrCAM is only required in glial cells (Feinberg, K., Eshed-Eisenbach, Y., Frechter, S., Amor, V., Salomon, D., Sabanay, H., Dupree, J. L., Grumet, M., Brophy, P. J., Shrager, P., and Peles, E. (2010) Neuron 65, 490-502). The olfactomedin domain of Gldn is implicated in the interaction with nodal Ig-CAMs. However, the interacting modules of NrCAM or NF186 involved in Gldn association are unknown. Here, we report that fibronectin type III-like (FnIII) domains of both Ig-CAMs mediate their interaction with Gldn in pulldown and cell binding assays. Using surface plasmon resonance assays, we determined that NrCAM and NF186 display similar affinity constant for their association with Gldn (K(D) of 0.9 and 5.7 nm, respectively). We characterized the FnIII domains 1 and 2 of NF186 as interacting modules that ensure association with Gldn. We found that the soluble FnIII domains of NF186 (FnIII-Fc) bind on Schwann cells and inhibit Gldn and Nav clustering at heminodes, the precursors of mature nodes in myelinating cultures. Our study reveals the unexpected importance of FnIII domains of Ig-CAMs in the organization of nodes of Ranvier in peripheral axons. Thus, NF186 utilizes distinct modules to organize the multimeric nodal complex. |
| Databáze: | OpenAIRE |
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