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Ankyrin 3, node of Ranvier

ankyrin-G, ANK3
Ankyrins are a family of proteins that are believed to link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact, and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 3 is an immunologically distinct gene product from ankyrins 1 and 2, and was originally found at the axonal initial segment and nodes of Ranvier of neurons in the central and peripheral nervous systems. Multiple transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Feb 2011] (from NCBI)
Top mentioned proteins: Neurofascin, Cav1.2, CAN, NODAL, ankyrin-B
Papers on ankyrin-G
Nanoscale Architecture of the Axon Initial Segment Reveals an Organized and Robust Scaffold.
Dargent et al., Marseille, France. In Cell Rep, Jan 2016
AIS assembly depends on a ßIV-spectrin/ankyrin G scaffold, but its macromolecular arrangement is not well understood.
An Adaptable Spectrin/Ankyrin-Based Mechanism for Long-Range Organization of Plasma Membranes in Vertebrate Tissues.
Lorenzo et al., Durham, United States. In Curr Top Membr, Dec 2015
In addition to protein interactions, cellular targeting and assembly of spectrin/ankyrin domains also critically depend on palmitoylation of ankyrin-G by aspartate-histidine-histidine-cysteine 5/8 palmitoyltransferases, as well as interaction of beta-2 spectrin with phosphoinositide lipids.
Isoforms of Spectrin and Ankyrin Reflect the Functional Topography of the Mouse Kidney.
Morrow et al., New Haven, United States. In Plos One, Dec 2015
Ankyrin G is the most abundant ankyrin, found in capillary endothelial cells and all tubular segments.
A Loss-of-Function Variant in a Minor Isoform of ANK3 Protects Against Bipolar Disorder and Schizophrenia.
Djurovic et al., Stockholm, Sweden. In Biol Psychiatry, Dec 2015
BACKGROUND: Ankyrin-3 (ANK3) was one of the first genes to reach significance in a bipolar disorder genome-wide association study.
What is the impact of genome-wide supported risk variants for schizophrenia and bipolar disorder on brain structure and function? A systematic review.
Prata et al., London, United Kingdom. In Psychol Med, Sep 2015
Irrespective of imaging modality, studies addressing the effect of SZ/BD GWAS risk genes (ANK3, CACNA1C, MHC, TCF4, NRGN, DGKH, PBRM1, NCAN and ZNF804A) were included.
Molecular neurobiological clues to the pathogenesis of bipolar disorder.
Harrison, Oxford, United Kingdom. In Curr Opin Neurobiol, Aug 2015
Recent genome-wide association studies have identified the first loci, implicating genes such as CACNA1C and ANK3.
Protein assemblies of sodium and inward rectifier potassium channels control cardiac excitability and arrhythmogenesis.
Jalife et al., Madrid, Spain. In Am J Physiol Heart Circ Physiol, Jul 2015
Recent findings include compartmentalized regulation of NaV1.5 channel expression and function through a PDZ (postsynaptic density protein, Drosophila disc large tumor suppressor, and zonula occludens-1 protein) domain-binding motif, and interaction of caveolin-3 with Kir2.1 and ankyrin-G as a molecular platform for NaV1.5 signaling.
Bioinformatics approach to predict target genes for dysregulated microRNAs in hepatocellular carcinoma: study on a chemically-induced HCC mouse model.
Tessitore et al., L'Aquila, Italy. In Bmc Bioinformatics, 2014
The expression of one (ANK3) among the 15 predicted targets was further validated by immunoblotting.
[New insights on the organization of the nodes of Ranvier].
Devaux, Marseille, France. In Rev Neurol (paris), 2014
This complex is essential for the recruitment of ankyrin-G, a cytoskeletal scaffolding protein, which binds and concentrates Nav channels at nodes.
New developments in the genetics of bipolar disorder.
Potash et al., Iowa City, United States. In Curr Psychiatry Rep, 2014
These have resulted in findings in genes including ANK3, CACNA1C, SYNE1, ODZ4, and TRANK1.
Bipolar disorder ANK3 risk variant effect on sustained attention is replicated in a large healthy population.
Stefanis et al., Athens, Greece. In Psychiatr Genet, 2012
Individuals carrying the bipolar disorder risk T-allele of ANK3 showed significantly reduced sensitivity in target detection, increased errors of commission, and atypical response latency variability.
A distal axonal cytoskeleton forms an intra-axonal boundary that controls axon initial segment assembly.
Rasband et al., Houston, United States. In Cell, 2012
AnkyrinG (ankG) is highly enriched in neurons at axon initial segments (AISs) where it clusters Na(+) and K(+) channels and maintains neuronal polarity.
An ankyrinG-binding motif is necessary and sufficient for targeting Nav1.6 sodium channels to axon initial segments and nodes of Ranvier.
Dib-Hajj et al., New Haven, United States. In J Neurosci, 2012
the ankyrinGbinding motif is both necessary and sufficient for the clustering of sodium channels at nodes of Ranvier and the AIS.
Sequencing chromosomal abnormalities reveals neurodevelopmental loci that confer risk across diagnostic boundaries.
Gusella et al., Boston, United States. In Cell, 2012
We sequenced BCAs in patients with autism or related NDDs, revealing disruption of 33 loci in four general categories: (1) genes previously associated with abnormal neurodevelopment (e.g., AUTS2, FOXP1, and CDKL5), (2) single-gene contributors to microdeletion syndromes (MBD5, SATB2, EHMT1, and SNURF-SNRPN), (3) novel risk loci (e.g., CHD8, KIRREL3, and ZNF507), and (4) genes associated with later-onset psychiatric disorders (e.g., TCF4, ZNF804A, PDE10A, GRIN2B, and ANK3).
Sequencing of the ANKYRIN 3 gene (ANK3) encoding ankyrin G in bipolar disorder reveals a non-conservative amino acid change in a short isoform of ankyrin G.
Gurling et al., London, United Kingdom. In Am J Med Genet B Neuropsychiatr Genet, 2012
DNA sequencing revealed a novel low frequency (0.007) ANK3 SNP (ss469104599) which causes a non-conservative amino acid change at position 794 in the shorter isoforms of the ankyrin G protein.
Connexin43 regulates sodium current; ankyrin-G modulates gap junctions: the intercalated disc exchanger.
Delmar, In Cardiovasc Res, 2012
loss of AnkG expression may prevent the arrival of Cx43 to its final destination.
Association analysis of ANK3 gene variants in nordic bipolar disorder and schizophrenia case-control samples.
Andreassen et al., Oslo, Norway. In Am J Med Genet B Neuropsychiatr Genet, 2011
These results further support that ANK3 is a susceptibility gene specific to bipolar disorder and that more than one risk locus is involved.
Genome-wide association study identifies five new schizophrenia loci.
Schizophrenia Psychiatric Genome-Wide Association Study (GWAS) Consortium, Boston, United States. In Nat Genet, 2011
In a joint analysis with a bipolar disorder sample (16,374 affected individuals and 14,044 controls), three loci reached genome-wide significance: CACNA1C (rs4765905, P = 7.0 × 10(-9)), ANK3 (rs10994359, P = 2.5 × 10(-8)) and the ITIH3-ITIH4 region (rs2239547, P = 7.8 × 10(-9)).
A selective filter for cytoplasmic transport at the axon initial segment.
Poo et al., Shanghai, China. In Cell, 2009
In cultured hippocampal neurons, we observed an ankyrin G- and F-actin-dependent structure that emerged in the cytoplasm of the axon initial segment (AIS) within 2 days after axon/dendrite differentiation, imposing a selective filter for diffusion of macromolecules and transport of vesicular carriers into the axon.
Ankyrin-G promotes cyclic nucleotide-gated channel transport to rod photoreceptor sensory cilia.
Bennett et al., Durham, United States. In Science, 2009
we report targeting of cyclic nucleotide-gated channel(CNG) to rod outer segment required interaction with ankyrin-G; ankyrin-G localized to rod outer segments, coimmunoprecipitated with CNG channel & bound to C-terminal domain of channel beta1 subunit
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