A regulated switch of chick neurofascin isoforms modulates ligand recognition and neurite extension

Pruss, Thomas; Kranz, Eva Ursula; Niere, Marc; Volkmer, Hansjürgen

doi:10.1016/j.mcn.2005.10.009

Cited by 20 publications

(28 citation statements)

References 47 publications

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“…The idea that NF first travels to the axon generally from the secretory pathway is also suggested by the transient broad axonal localization of NF in very young stage 3 neurons (phase IS1). An early axonal targeting might account for the proposed roles of NF and NrCAM in axon outgrowth and pathfinding in the chick and mouse visual system (Sakurai et al, 2001;Pruss et al, 2004Pruss et al, , 2006Zelina et al, 2005;Williams et al, 2006). After axon outgrowth and synaptogenesis are complete, secretory IS targeting might develop as a mature mechanism to efficiently enrich IS components at the IS later on.…”

Section: Neurofascin Accumulation In the Is During Axonogenesismentioning

confidence: 99%

Ankyrin-Dependent and -Independent Mechanisms Orchestrate Axonal Compartmentalization of L1 Family Members Neurofascin and L1/Neuron–Glia Cell Adhesion Molecule

Boiko¹,

Vakulenko²,

Ewers³

et al. 2007

J. Neurosci.

114

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Axonal initial segments (IS) and nodes of Ranvier are functionally important membrane subdomains in which the clustering of electrogenic channels enables action potential initiation and propagation. In addition, the initial segment contributes to neuronal polarity by serving as a diffusion barrier. To study the mechanisms of axonal compartmentalization, we focused on two L1 family of cell adhesion molecules (L1-CAMs) [L1/neuron-glia cell adhesion molecule (L1/NgCAM) and neurofascin (NF)] and two neuronal ankyrins (ankB and ankG). NF and ankG accumulate specifically at the initial segment, whereas L1/NgCAM and ankB are expressed along the entire lengths of axons. We find that L1/NgCAM and NF show distinct modes of steady-state accumulation during axon outgrowth in cultured hippocampal neurons. Despite their different steady-state localizations, both L1/NgCAM and NF show slow diffusion and low detergent extractability specifically in the initial segment but fast diffusion and high detergent extractability in the distal axon. We propose that L1-CAMs do not strongly bind ankB in the distal axon because of spatial regulation of ankyrin affinity by phosphorylation. NF, conversely, is initially enriched in an ankyrin-independent manner in the axon generally and accumulates progressively in the initial segment attributable to preferential binding to ankG. Our results suggest that NF and L1/NgCAM accumulate in the axon by an ankyrinindependent pathway, but retention at the IS requires ankyrin binding.

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Section: Neurofascin Accumulation In the Is During Axonogenesismentioning

confidence: 99%

Ankyrin-Dependent and -Independent Mechanisms Orchestrate Axonal Compartmentalization of L1 Family Members Neurofascin and L1/Neuron–Glia Cell Adhesion Molecule

Boiko¹,

Vakulenko²,

Ewers³

et al. 2007

J. Neurosci.

114

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“…Plasmids and Antibodies-cDNA expression vectors for chick neurofascin isoforms NF166 and NF186 as well as the NF166-CD and -ED mutants were described previously (7,10). NF166 point mutants and COOH-terminally truncated variants were constructed with the help of a QuikChange mutagenesis kit (Stratagene, Heidelberg, Germany).…”

Section: Methodsmentioning

confidence: 99%

“…Immunocytochemistry of chick neurons and immunoprecipitation of chick NF166-ED were carried out with a polyclonal anti-chick neurofascin antibody that recognized the extracellular domain of chick neurofascin (7). FGFR1 peptides derived from rat brain were detected by polyclonal antibodies (Abcam, Cambridge, UK), whereas a monoclonal antibody was applied for recombinant mouse FGFR1 (Upstate Technologies, Dundee, UK).…”

Section: Methodsmentioning

confidence: 99%

“…PC12-E2 cells (7,21) were grown in a humidified atmosphere containing 10% CO 2 at 37°C in Dulbecco's modified Eagle's medium supplemented with 10% (v/v) heat-inactivated horse serum (Invitrogen), 5% (v/v) heat-inactivated fetal calf serum, 2 mM glutamine, 100 units/ml penicillin, 100 g/ml streptomycin, and 100 g/ml G418 (PAA, Pasching, Austria). NIH/3T3 and HEK293 cells were maintained in Dulbecco's modified Eagle's medium supplemented with 10% (v/v) fetal calf serum, 2 mM glutamine, 100 units/ml penicillin, and 100 g/ml streptomycin in a humidified atmosphere containing 5% CO 2 at 37°C.…”

Section: Methodsmentioning

confidence: 99%

“…Different alternatively spliced neurofascin isoforms are expressed in different cells and at different times of development (6). Embryonal neurofascin NF166 is important for neurite outgrowth and guidance (7,8). Recently, a role for neurofascin NF166 for early processes of inhibitory synaptogenesis at the axon hillock and for the positioning of inhibitory synapses at the axon initial segment has been proven (9,10).…”

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confidence: 99%

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Analysis of Non-canonical Fibroblast Growth Factor Receptor 1 (FGFR1) Interaction Reveals Regulatory and Activating Domains of Neurofascin

Kirschbaum

Kriebel

Kranz

et al. 2009

Journal of Biological Chemistry

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Fibroblast growth factor receptors (FGFRs) are important for many different mechanisms, including cell migration, proliferation, differentiation, and survival. Here, we show a new link between FGFR1 and the cell adhesion molecule neurofascin, which is important for neurite outgrowth. After overexpression in HEK293 cells, embryonal neurofascin isoform NF166 was able to associate with FGFR1, whereas the adult isoform NF186, differing from NF166 in additional extracellular sequences, was deficient. Pharmacological inhibitors and overexpression of dominant negative components of the FGFR signaling pathway pointed to the activation of FGFR1 after association with neurofascin in neurite outgrowth assays in chick tectal neurons and rat PC12-E2 cells. Both extra-and intracellular domains of embryonal neurofascin isoform NF166 were able to form complexes with FGFR1 independently. However, the cytosolic domain was both necessary and sufficient for the activation of FGFR1. Cytosolic serine residues 56 and 100 were shown to be essential for the neurite outgrowth-promoting activity of neurofascin, whereas both amino acid residues were dispensable for FGFR1 association. In conclusion, the data suggest a neurofascin intracellular domain, which activates FGFR1 for neurite outgrowth, whereas the extracellular domain functions as an additional, regulatory FGFR1 interaction domain in the course of development.The four known fibroblast growth factor receptors (FGFRs), 2 which are targeted by a large family of 22 fibroblast growth factor ligands, represent a highly diverse signaling system important for migration, proliferation, differentiation, and survival of many different cell types (1, 2). fibroblast growth factor activation of FGFR leads to the activation of mitogen-activated protein kinase (MAPK), phosphatidylinositol 3-kinase (PI3K), and phospholipase C␥ (PLC␥), depending on the cellular system under study. Non-canonical FGFR interactions with NCAM, cadherins, and syndecan via extracellular domains were also described (1). However, the contribution of intracellular interactions of FGFR1 with further membrane co-receptors is poorly understood. Only cytosolic interaction between FGFRs and EphA4 have been described that are involved in mutual transphosphorylation (3).The cell adhesion molecule neurofascin is important for cellcell communication in the nervous system (4, 5). Neurofascin regulates many different functions in the brain, suggesting that it functions as a key regulator for both developing and differentiated neural cells. Different alternatively spliced neurofascin isoforms are expressed in different cells and at different times of development (6). Embryonal neurofascin NF166 is important for neurite outgrowth and guidance (7,8). Recently, a role for neurofascin NF166 for early processes of inhibitory synaptogenesis at the axon hillock and for the positioning of inhibitory synapses at the axon initial segment has been proven (9, 10).In the more developed nervous system, NF166 is replaced by NF186, which is inhibitory...

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The immunoglobulin superfamily of neuronal cell adhesion molecules: Lessons from animal models and correlation with human disease

Κατίδου

Vidaki

Strigini

et al. 2008

Biotechnology Journal

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Neuronal cell adhesion molecules of the immunoglobulin superfamily (IgCAMs) play a crucial role in the formation of neural circuits at different levels: cell migration, axonal and dendritic targeting as well as synapse formation. Furthermore, in perinatal and adult life, neuronal IgCAMs are required for the formation and maintenance of specialized axonal membrane domains, synaptic plasticity and neurogenesis. Mutations in the corresponding human genes have been correlated to several human neuronal disorders. Perturbing neuronal IgCAMs in animal models provides powerful means to understand the molecular and cellular basis of such human disorders. In this review, we concentrate on the NCAM, L1 and contactin subfamilies of neuronal IgCAMs summarizing recent functional studies from model systems and highlighting their links to disease pathogenesis.

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A regulated switch of chick neurofascin isoforms modulates ligand recognition and neurite extension

Cited by 20 publications

References 47 publications

Ankyrin-Dependent and -Independent Mechanisms Orchestrate Axonal Compartmentalization of L1 Family Members Neurofascin and L1/Neuron–Glia Cell Adhesion Molecule

Ankyrin-Dependent and -Independent Mechanisms Orchestrate Axonal Compartmentalization of L1 Family Members Neurofascin and L1/Neuron–Glia Cell Adhesion Molecule

Analysis of Non-canonical Fibroblast Growth Factor Receptor 1 (FGFR1) Interaction Reveals Regulatory and Activating Domains of Neurofascin

The immunoglobulin superfamily of neuronal cell adhesion molecules: Lessons from animal models and correlation with human disease

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