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    Ank1 ankyrin 1, erythroid [ Mus musculus (house mouse) ]

    Gene ID: 11733, updated on 21-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Ankyrin-R regulates fast-spiking interneuron excitability through perineuronal nets and Kv3.1b K(+) channels.

    Ankyrin-R regulates fast-spiking interneuron excitability through perineuronal nets and Kv3.1b K(+) channels.
    Stevens SR, Longley CM, Ogawa Y, Teliska LH, Arumanayagam AS, Nair S, Oses-Prieto JA, Burlingame AL, Cykowski MD, Xue M, Rasband MN., Free PMC Article

    10/9/2021
    Parasites in ankyrin-1 (Ank-1) mutation erythrocytes grew normally, but red cells showed resistance to merozoite invasion.

    A novel ENU-induced ankyrin-1 mutation impairs parasite invasion and increases erythrocyte clearance during malaria infection in mice.
    Huang HM, Bauer DC, Lelliott PM, Greth A, McMorran BJ, Foote SJ, Burgio G., Free PMC Article

    07/7/2018
    This study highlights the first direct examination of allelic heterogeneity of the Ank-1 gene in the context of malaria resistance in mouse models.

    Ankyrin-1 Gene Exhibits Allelic Heterogeneity in Conferring Protection Against Malaria.
    Huang HM, Bauer DC, Lelliott PM, Dixon MWA, Tilley L, McMorran BJ, Foote SJ, Burgio G., Free PMC Article

    05/5/2018
    With increasing age (at 12-15 mo of age) extensor digitorum longus (EDL) skeletal muscles of sAnk1 KO mice develop prematurely large tubular aggregates.

    Deletion of small ankyrin 1 (sAnk1) isoforms results in structural and functional alterations in aging skeletal muscle fibers.
    Giacomello E, Quarta M, Paolini C, Squecco R, Fusco P, Toniolo L, Blaauw B, Formoso L, Rossi D, Birkenmeier C, Peters LL, Francini F, Protasi F, Reggiani C, Sorrentino V.

    03/21/2015
    Study shows a direct interaction between beta-III spectrin and erythroid ankyrin in the cerebellum and to demonstrate a critical role for beta-III spectrin in maintaining ankyrin R throughout the Purkinje cell dendritic tree.

    β-III spectrin underpins ankyrin R function in Purkinje cell dendritic trees: protein complex critical for sodium channel activity is impaired by SCA5-associated mutations.
    Clarkson YL, Perkins EM, Cairncross CJ, Lyndon AR, Skehel PA, Jackson M., Free PMC Article

    02/14/2015
    Hema6 mutation of ankyrin-1 causes hereditary spherocytosis in mice through a mild reduction of protein expression.

    A deep intronic mutation in the ankyrin-1 gene causes diminished protein expression resulting in hemolytic anemia in mice.
    Huang H, Zhao P, Arimatsu K, Tabeta K, Yamazaki K, Krieg L, Fu E, Zhang T, Du X., Free PMC Article

    06/28/2014
    Suppression of hepcidin expression and iron overload mediate Salmonella susceptibility in ankyrin 1-mutated mice.

    Suppression of hepcidin expression and iron overload mediate Salmonella susceptibility in ankyrin 1 ENU-induced mutant.
    Yuki KE, Eva MM, Richer E, Chung D, Paquet M, Cellier M, Canonne-Hergaux F, Vaulont S, Vidal SM, Malo D., Free PMC Article

    07/20/2013
    We conclude that increased malaria resistance due to ankyrin-1 deficiency is caused by the intraerythrocytic death of P. chabaudi parasites.

    A novel ENU-mutation in ankyrin-1 disrupts malaria parasite maturation in red blood cells of mice.
    Greth A, Lampkin S, Mayura-Guru P, Rodda F, Drysdale K, Roberts-Thomson M, McMorran BJ, Foote SJ, Burgio G., Free PMC Article

    12/22/2012
    These results demonstrate that mammalian erythroblast enucleation does not depend on the membrane integrity generated by the ankyrin-band 3 complex.

    Ankyrin and band 3 differentially affect expression of membrane glycoproteins but are not required for erythroblast enucleation.
    Ji P, Lodish HF., Free PMC Article

    04/7/2012
    The Ank1(E924X) strain provides a novel tool to study Ank1 and model HS.

    A novel ENU-generated truncation mutation lacking the spectrin-binding and C-terminal regulatory domains of Ank1 models severe hemolytic hereditary spherocytosis.
    Hughes MR, Anderson N, Maltby S, Wong J, Berberovic Z, Birkenmeier CS, Haddon DJ, Garcha K, Flenniken A, Osborne LR, Adamson SL, Rossant J, Peters LL, Minden MD, Paulson RF, Wang C, Barber DL, McNagny KM, Stanford WL., Free PMC Article

    04/23/2011
    Mice homozygous for the Ank-1 mutation are profoundly anemic in utero and most die perinatally, indicating that Ank-1 plays a nonredundant role in erythroid development.

    Novel roles for erythroid Ankyrin-1 revealed through an ENU-induced null mouse mutant.
    Rank G, Sutton R, Marshall V, Lundie RJ, Caddy J, Romeo T, Fernandez K, McCormack MP, Cooke BM, Foote SJ, Crabb BS, Curtis DJ, Hilton DJ, Kile BT, Jane SM., Free PMC Article

    01/21/2010
    the organization of obscurin at different locations in the sarcomere changes during muscle development and that this might affect the interaction with ank1.5.

    Localization of ank1.5 in the sarcoplasmic reticulum precedes that of SERCA and RyR: relationship with the organization of obscurin in developing sarcomeres.
    Giacomello E, Sorrentino V.

    01/21/2010
    A spontaneous mutation, normoblastosis (Ank1nb) in mice provides an important animal model for human ankyrin-deficient anemias.

    Normoblastosis, a murine model for ankyrin-deficient hemolytic anemia, is caused by a hypomorphic mutation in the erythroid ankyrin gene Ank1.
    Birkenmeier CS, Gifford EJ, Barker JE.

    01/21/2010
    Results support a role of obscurin in mediating the subcellular localization of small ankyrin1 isoforms in striated muscle cells.

    Molecular interactions with obscurin are involved in the localization of muscle-specific small ankyrin1 isoforms to subcompartments of the sarcoplasmic reticulum.
    Armani A, Galli S, Giacomello E, Bagnato P, Barone V, Rossi D, Sorrentino V.

    01/21/2010
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