| First Author | Hayashi C | Year | 2020 |
| Journal | Biochem Biophys Res Commun | Volume | 523 |
| Issue | 1 | Pages | 171-176 |
| PubMed ID | 31839217 | Mgi Jnum | J:292702 |
| Mgi Id | MGI:6445076 | Doi | 10.1016/j.bbrc.2019.12.002 |
| Citation | Hayashi C, et al. (2020) The extracellular domain of teneurin-4 promotes cell adhesion for oligodendrocyte differentiation. Biochem Biophys Res Commun 523(1):171-176 |
| abstractText | Cell adhesion between oligodendrocytes and neuronal axons is a critical step for myelination that enables the rapid propagation of action potential in the central nervous system. Here, we show that the transmembrane protein teneurin-4 plays a role in the cell adhesion required for the differentiation of oligodendrocytes. We found that teneurin-4 formed molecular complexes with all of the four teneurin family members and promoted cell-cell adhesion. Oligodendrocyte lineage cells attached to the recombinant extracellular domain of all the teneurins and formed well-branched cell processes. In an axon-mimicking nanofibers assay, nanofibers coated with the recombinant teneurin-4 extracellular domain increased the differentiation of oligodendrocytes. Our results show that teneurin-4 binds to all teneurins through their extracellular domain, which facilitates the oligodendrocyte-axon adhesion, and promotes oligodendrocyte differentiation via its homophilic interaction. |
