Topic
Paranodal junction
About: Paranodal junction is a research topic. Over the lifetime, 117 publications have been published within this topic receiving 18375 citations.
Papers published on a yearly basis
Papers
TL;DR: The co-localization of two Shaker-like voltage-gated K+-channel proteins is described, indicating that the two polypeptides occur in subcellular regions where rapid membrane repolarization may be important and that they form heteromultimeric channels in vivo.
Abstract: Voltage-gated potassium (K+) channels display a wide variety of conductances and gating properties in vivo This diversity can be attributed not only to the presence of many K(+)-channel gene products, but also to the possibility that different K(+)-channel subunits co-assemble to form heteromultimeric channels in vivo When expressed in Xenopus oocytes or transfected cells, K(+)-channel polypeptides assemble to form tetramers Certain combinations of Shaker-like subunits have been shown to co-assemble, forming heteromultimeric channels with distinct properties It is not known, however, whether K(+)-channel polypeptides form heteromultimeric channels in vivo Here we describe the co-localization of two Shaker-like voltage-gated K(+)-channel proteins, mKv11 and mKv12, in the juxtaparanodal regions of nodes of Ranvier in myelinated axons, and in terminal fields of basket cells in mouse cerebellum We also show that mKv11 and mKv12 can be coimmunoprecipitated with specific antibodies that recognize only one of them These data indicate that the two polypeptides occur in subcellular regions where rapid membrane repolarization may be important and that they form heteromultimeric channels in vivo
667 citations
TL;DR: Results indicate that GalC and sulfatide play important roles in myelin function and stability.
650 citations
TL;DR: It is demonstrated that ankyrinG is essential for clustering NaCh and neurofascin at axon initial segments and is required for physiological levels of sodium channel activity.
Abstract: Voltage-gated sodium channels (NaCh) are colocalized with isoforms of the membrane-skeletal protein ankyrinG at axon initial segments, nodes of Ranvier, and postsynaptic folds of the mammalian neuromuscular junction. The role of ankyrinG in directing NaCh localization to axon initial segments was evaluated by region-specific knockout of ankyrinG in the mouse cerebellum. Mutant mice exhibited a progressive ataxia beginning around postnatal day P16 and subsequent loss of Purkinje neurons. In mutant mouse cerebella, NaCh were absent from axon initial segments of granule cell neurons, and Purkinje cells showed deficiencies in their ability to initiate action potentials and support rapid, repetitive firing. Neurofascin, a member of the L1CAM family of ankyrin-binding cell adhesion molecules, also exhibited impaired localization to initial segments of Purkinje cell neurons. These results demonstrate that ankyrinG is essential for clustering NaCh and neurofascin at axon initial segments and is required for physiological levels of sodium channel activity.
603 citations
TL;DR: Results show a critical role for NCP1 in the delineation of specific axonal domains and the axon-glia interactions required for normal saltatory conduction.
589 citations
TL;DR: It is demonstrated that Caspr2 and TAG-1 form a scaffold that is necessary to maintain K+ channels at the juxtaparanodal region, suggesting that axon–glia interactions mediated by these proteins allow myelinating glial cells to organize ion channels in the underlying axonal membrane.
Abstract: In myelinated axons, K+ channels are concealed under the myelin sheath in the juxtaparanodal region, where they are associated with Caspr2, a member of the neurexin superfamily. Deletion of Caspr2 in mice by gene targeting revealed that it is required to maintain K+ channels at this location. Furthermore, we show that the localization of Caspr2 and clustering of K+ channels at the juxtaparanodal region depends on the presence of TAG-1, an immunoglobulin-like cell adhesion molecule that binds Caspr2. These results demonstrate that Caspr2 and TAG-1 form a scaffold that is necessary to maintain K+ channels at the juxtaparanodal region, suggesting that axon–glia interactions mediated by these proteins allow myelinating glial cells to organize ion channels in the underlying axonal membrane.
570 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 1 |
| 2020 | 3 |
| 2019 | 3 |
| 2018 | 5 |
| 2017 | 2 |
| 2016 | 1 |