gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Ankyrin 2, neuronal

ankyrin-B, ANK2, LQT4, ankyrin 2
This gene encodes a member of the ankyrin family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton. Ankyrins play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. 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. The protein encoded by this gene is required for targeting and stability of Na/Ca exchanger 1 in cardiomyocytes. Mutations in this gene cause long QT syndrome 4 and cardiac arrhythmia syndrome. Multiple transcript variants encoding different isoforms have been described. [provided by RefSeq, Dec 2011] (from NCBI)
Top mentioned proteins: SCN5A, ankyrin-G, HERG, CAN, KCNQ1
Papers on ankyrin-B
Ankyrin-B directs membrane tethering of periaxin and is required for maintenance of lens fiber cell hexagonal shape and mechanics.
Rao et al., Edinburgh, United Kingdom. In Am J Physiol Cell Physiol, Feb 2016
Here we report that ankyrin-B (AnkB), a well-characterized adaptor protein involved in linking the spectrin-actin cytoskeleton to integral membrane proteins, is required for membrane association of Prx in lens fibers and colocalizes with Prx in hexagonal fiber cells.
Identification of a VxP Targeting Signal in the Flagellar Na(+) /K(+) -ATPase.
Baker et al., Iowa City, United States. In Traffic, Dec 2015
In the retina, NKA and ankyrin-B are expressed in multiple cell types and immunostaining for each is striking in the synaptic layers.
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 B populates Bowman's capsule, podocytes, the ascending thick loop of Henle, and the distal convoluted tubule.
Identification and characterization of two ankyrin-B isoforms in mammalian heart.
Cunha et al., Houston, United States. In Cardiovasc Res, Oct 2015
CONCLUSION: The identification and characterization of two functionally distinct ankyrin-B isoforms in heart provide compelling evidence that alternative splicing of the ANK2 gene regulates the fidelity of ankyrin-B interactions with proteins.
Targeted next generation sequencing application in cardiac channelopathies: Analysis of a cohort of autopsy-negative sudden unexplained deaths.
Ludes et al., Strasbourg, France. In Forensic Sci Int, Sep 2015
However, after the prioritization process using a new scoring program (VaRank) and after the conjunction of clinical data and molecular findings, four "likely pathogenic" variants (including two undescribed variants), were identified in three cases (18.75%) of our cohort in the genes KCNH2, ANK2, SCN5A and RYR2.
Ankyrin-B metabolic syndrome combines age-dependent adiposity with pancreatic β cell insufficiency.
Bennett et al., In J Clin Invest, Sep 2015
Rare functional variants of ankyrin-B have been implicated in human disease, including hereditary cardiac arrhythmia and type 2 diabetes (T2D).
Genetic Analysis of Arrhythmogenic Diseases in the Era of NGS: The Complexity of Clinical Decision-Making in Brugada Syndrome.
Brugada et al., Girona, Spain. In Plos One, 2014
Twenty-eight genes were resequenced: AKAP9, ANK2, CACNA1C, CACNB2, CASQ2, CAV3, DSC2, DSG2, DSP, GPD1L, HCN4, JUP, KCNE1, KCNE2, KCNE3, KCNH2, KCNJ2, KCNJ5, KCNQ1, NOS1AP, PKP2, RYR2, SCN1B, SCN3B, SCN4B, SCN5A, SNTA1, and TMEM43.
Genetics of long QT syndrome.
Ackerman et al., Rochester, United States. In Methodist Debakey Cardiovasc J, 2014
In addition, three atypical LQTS or multisystem syndromic disorders that have been associated with QT prolongation have been described, including ankyrin-B syndrome, Anderson-Tawil syndrome (ATS), and Timothy syndrome (TS).
Ankyrin-B protein in heart failure: identification of a new component of metazoan cardioprotection.
Mohler et al., Columbus, United States. In J Biol Chem, 2012
Ankyrin-B protein in heart failure: identification of a new component of metazoan cardioprotection.
From global to local: a new understanding of cardiac electromechanical coupling.
Swift et al., Oslo, Norway. In Tidsskr Nor Laegeforen, 2012
The significance of the binding protein ankyrin-B and the Ca2+ channel IP3R (inositol 1,4,5-triphosphate receptor) is best understood in this context.
Ankyrin-B reduction enhances Ca spark-mediated SR Ca release promoting cardiac myocyte arrhythmic activity.
Despa et al., Davis, United States. In J Mol Cell Cardiol, 2012
AnkB reduction alters cardiac Na and Ca transport and enhances the coupled RyR openings, resulting in more frequent Ca sparks and waves although the total SR Ca leak is unaffected.
Exploitation of evolutionarily conserved amoeba and mammalian processes by Legionella.
Abu Kwaik et al., Louisville, United States. In Trends Microbiol, 2012
This is highlighted by the ankyrin B (AnkB) F-box effector that exploits multiple conserved eukaryotic machineries to generate high levels of free amino acids as sources of carbon and energy essential for intracellular proliferation in protists and metazoan cells and for manifestation of pulmonary disease in mammals.
A distal axonal cytoskeleton forms an intra-axonal boundary that controls axon initial segment assembly.
Rasband et al., Houston, United States. In Cell, 2012
Here, we show that as neurons break symmetry, they assemble a distal axonal submembranous cytoskeleton, comprised of ankyrinB (ankB), αII-spectrin, and βII-spectrin, that defines a boundary limiting ankG to the proximal axon.
Defects in ankyrin-based membrane protein targeting pathways underlie atrial fibrillation.
Mohler et al., Columbus, United States. In Circulation, 2011
Reduced ankyrin-B expression or mutations in ankyrin 2 are associated with atrial fibrillation.
Beyond membrane channelopathies: alternative mechanisms underlying complex human disease.
Mohler et al., Columbus, United States. In Acta Pharmacol Sin, 2011
For example, over the past few years, a new class of potentially fatal cardiac arrhythmias has been linked with cytoplasmic proteins that include sub-membrane adapters such as ankyrin-B (ANK2), ankyrin-G (ANK3), and alpha-1 syntrophin, membrane coat proteins including caveolin-3 (CAV3), signaling platforms including yotiao (AKAP9), and cardiac enzymes (GPD1L).
Ankyrin-B interactions with spectrin and dynactin-4 are required for dystrophin-based protection of skeletal muscle from exercise injury.
Bennett et al., Durham, United States. In J Biol Chem, 2011
Ankyrin-B then interacts with dynactin-4 and dystrophin, whereas dynactin-4 collaborates with dystrophin in coordinating costamere-aligned microtubules
Ankyrin-B regulates Kir6.2 membrane expression and function in heart.
Mohler et al., Iowa City, United States. In J Biol Chem, 2010
Ankyrin-B regulates Kir6.2 membrane expression and function in heart.
An ankyrin-based mechanism for functional organization of dystrophin and dystroglycan.
Bennett et al., Durham, United States. In Cell, 2009
Ankyrin-B thus is an adaptor required for sarcolemmal localization of dystrophin, as well as dynactin-4.
Long QT Syndrome
Christiaans et al., Seattle, United States. In Unknown Journal, 2003
Other, less frequently involved genes are ANK2 (LQT4), KCNE1 (LQT5), KCNE2 (LQT6), KCNJ2 (LQT7), CACNA1C (LQT8), CAV3 (LQT9), SCN4B (LQT10), AKAP9 (LQT11), SNTA1 (LQT12), KCNJ5 (LQT13), CALM1 (LQT14), and CALM2 (LQT15).
Ankyrin-B mutation causes type 4 long-QT cardiac arrhythmia and sudden cardiac death.
Bennett et al., Durham, United States. In Nature, 2003
Mice heterozygous for a null mutation in ankyrin-B are haploinsufficient and display arrhythmia similar to humans
share on facebooktweetadd +1mail to friends