Tyrosine phosphorylation at a site highly conserved in the L1 family of cell adhesion molecules abolishes ankyrin binding and increases lateral mobility of neurofascin.
about
The neural cell recognition molecule neurofascin interacts with syntenin-1 but not with syntenin-2, both of which reveal self-associating activitySpectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissuesPhosphorylation and ankyrin-G binding of the C-terminal domain regulate targeting and function of the ammonium transporter RhBGMAP kinase pathway-dependent phosphorylation of the L1-CAM ankyrin binding site regulates neuronal growthThe phosphorylation state of the FIGQY tyrosine of neurofascin determines ankyrin-binding activity and patterns of cell segregationAnkyrinG is required for clustering of voltage-gated Na channels at axon initial segments and for normal action potential firingAdducin is an in vivo substrate for protein kinase C: phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neuronsNeurofascin assembles a specialized extracellular matrix at the axon initial segmentSodium channel beta1 and beta3 subunits associate with neurofascin through their extracellular immunoglobulin-like domainWilling to Be Involved in CancerReciprocal Interactions between Cell Adhesion Molecules of the Immunoglobulin Superfamily and the Cytoskeleton in NeuronsCell Adhesion Molecules and Ubiquitination-Functions and SignificanceFunctional implications of axon initial segment cytoskeletal disruption in strokeAxon initial segments: diverse and dynamic neuronal compartmentsTranssynaptic coordination of synaptic growth, function, and stability by the L1-type CAM NeuroglianActivation of the MAPK signal cascade by the neural cell adhesion molecule L1 requires L1 internalization.Recycling of the cell adhesion molecule L1 in axonal growth cones.Interactions between the L1 cell adhesion molecule and ezrin support traction-force generation and can be regulated by tyrosine phosphorylation.Structural requirements for association of neurofascin with ankyrinSodium channel beta subunits: anything but auxiliaryStructural requirements for interaction of sodium channel beta 1 subunits with ankyrinThe role of endocytosis in regulating L1-mediated adhesionLAD-1, the Caenorhabditis elegans L1CAM homologue, participates in embryonic and gonadal morphogenesis and is a substrate for fibroblast growth factor receptor pathway-dependent phosphotyrosine-based signalingRestriction of 480/270-kD ankyrin G to axon proximal segments requires multiple ankyrin G-specific domainsAnalysis of non-canonical fibroblast growth factor receptor 1 (FGFR1) interaction reveals regulatory and activating domains of neurofascinEthanol causes the redistribution of L1 cell adhesion molecule in lipid raftsNodes of Ranvier and axon initial segments are ankyrin G-dependent domains that assemble by distinct mechanismsTyrosine-phosphorylated and nonphosphorylated sodium channel beta1 subunits are differentially localized in cardiac myocytesEndocytosis and endosomes at the crossroads of regulating trafficking of axon outgrowth-modifying receptors.Trafficking guidance receptorsFast turnover of L1 adhesions in neuronal growth cones involving both surface diffusion and exo/endocytosis of L1 molecules.Cloning and expression of a zebrafish SCN1B ortholog and identification of a species-specific splice variant.Novel forms of neurofascin 155 in the central nervous system: alterations in paranodal disruption models and multiple sclerosisMyelination and regional domain differentiation of the axon.Organization and maintenance of molecular domains in myelinated axonsChannelrhodopsin-2 localised to the axon initial segment.Nodes, paranodes, and incisures: from form to function.L1-mediated branching is regulated by two ezrin-radixin-moesin (ERM)-binding sites, the RSLE region and a novel juxtamembrane ERM-binding region.Genetic and clinical aspects of X-linked hydrocephalus (L1 disease): Mutations in the L1CAM gene.Obstructed diffusion in phase-separated supported lipid bilayers: a combined atomic force microscopy and fluorescence recovery after photobleaching approach.
P2860
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P2860
Tyrosine phosphorylation at a site highly conserved in the L1 family of cell adhesion molecules abolishes ankyrin binding and increases lateral mobility of neurofascin.
description
1997 nî lūn-bûn
@nan
1997 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Tyrosine phosphorylation at a ...... teral mobility of neurofascin.
@ast
Tyrosine phosphorylation at a ...... teral mobility of neurofascin.
@en
Tyrosine phosphorylation at a ...... teral mobility of neurofascin.
@nl
type
label
Tyrosine phosphorylation at a ...... teral mobility of neurofascin.
@ast
Tyrosine phosphorylation at a ...... teral mobility of neurofascin.
@en
Tyrosine phosphorylation at a ...... teral mobility of neurofascin.
@nl
prefLabel
Tyrosine phosphorylation at a ...... teral mobility of neurofascin.
@ast
Tyrosine phosphorylation at a ...... teral mobility of neurofascin.
@en
Tyrosine phosphorylation at a ...... teral mobility of neurofascin.
@nl
P2093
P2860
P356
P1476
Tyrosine phosphorylation at a ...... teral mobility of neurofascin.
@en
P2093
P2860
P304
P356
10.1083/JCB.137.3.703
P407
P577
1997-05-01T00:00:00Z