ArticleThe Journal of cell biology1998
Dissection of complex molecular interactions of neurofascin with axonin-1, F11, and tenascin-R, which promote attachment and neurite formation of tectal cells.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 99 citations in OpenAlex.
- Antibody-directed extracellular proximity biotinylation reveals that Contactin-1 regulates axo-axonic innervation of axon initial segments.Nature communications · 2023Article
- Structural insights into the contactin 1 - neurofascin 155 adhesion complex.Nature communications · 2022Article
- Early Days of Tenascin-R Research: Two Approaches Discovered and Shed Light on Tenascin-R.Frontiers in immunology · 2020Article
- Structural Perspectives on Extracellular Recognition and Conformational Changes of Several Type-I Transmembrane Receptors.Frontiers in molecular biosciences · 2020Review
- Article
- Specific contactin N-glycans are implicated in neurofascin binding and autoimmune targeting in peripheral neuropathies.The Journal of biological chemistry · 2014Article
- Contactin-1 regulates myelination and nodal/paranodal domain organization in the central nervous system.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Neuro-glial interactions at the nodes of Ranvier: implication in health and diseases.Frontiers in cellular neuroscience · 2013Review
- Protein tyrosine phosphatases PTPδ, PTPσ, and LAR: presynaptic hubs for synapse organization.Trends in neurosciences · 2013Review
- Regulation of adhesion by flexible ectodomains of IgCAMs.Neurochemical research · 2013Review
- Article
- Fibronectin type III-like domains of neurofascin-186 protein mediate gliomedin binding and its clustering at the developing nodes of Ranvier.The Journal of biological chemistry · 2011Article
- The cell adhesion molecule neurofascin stabilizes axo-axonic GABAergic terminals at the axon initial segment.The Journal of biological chemistry · 2011Article
- A spontaneous mutation in contactin 1 in the mouse.PloS one · 2011Article
- The expression of TAG-1 in glial cells is sufficient for the formation of the juxtaparanodal complex and the phenotypic rescue of tag-1 homozygous mutants in the CNS.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Brain extracellular matrix affects AMPA receptor lateral mobility and short-term synaptic plasticity.Nature neuroscience · 2009Article
- Versican V2 assembles the extracellular matrix surrounding the nodes of ranvier in the CNS.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- PGY repeats and N-glycans govern the trafficking of paranodin and its selective association with contactin and neurofascin-155.Molecular biology of the cell · 2007Article
- Caspr regulates the processing of contactin and inhibits its binding to neurofascin.The Journal of cell biology · 2003Article
- Retention of a cell adhesion complex at the paranodal junction requires the cytoplasmic region of Caspr.The Journal of cell biology · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neurofascin is a member of the L1 subgroup of the Ig superfamily that promotes axon outgrowth by interactions with neuronal NgCAM-related cell adhesion molecule (NrCAM). We used a combination of cellular binding assays and neurite outgrowth experiments to investigate mechanisms that might modulate the interactions of neurofascin. In addition to NrCAM, we here demonstrate that neurofascin also binds to the extracellular matrix glycoprotein tenascin-R (TN-R) and to the Ig superfamily members axonin-1 and F11. Isoforms of neurofascin that are generated by alternative splicing show different preferences in ligand binding. While interactions of neurofascin with F11 are only slightly modulated, binding to axonin-1 and TN-R is strongly regulated by alternatively spliced stretches located in the NH2-terminal half, and by the proline-alanine-threonine-rich segment. In vitro neurite outgrowth and cell attachment assays on a neurofascin-Fc substrate reveal a shift of cellular receptor usage from NrCAM to axonin-1, F11, and at least one additional protein in the presence of TN-R, presumably due to competition of the neurofascin- NrCAM interaction. Thereby, F11 binds to TN-R of the neurofascin/TN-R complex, but not to neurofascin, whereas axonin-1 is not able to bind directly to the neurofascin/TN-R complex as shown by competition binding assays. In conclusion, these investigations indicate that the molecular interactions of neurofascin are regulated at different levels, including alternative splicing and by the presence of interacting proteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.