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    Dtna dystrobrevin alpha [ Mus musculus (house mouse) ]

    Gene ID: 13527, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Plasticity and structural alterations of mitochondria and sarcoplasmic organelles in muscles of mice deficient in alpha-dystrobrevin, a component of the dystrophin-glycoprotein complex.

    Plasticity and structural alterations of mitochondria and sarcoplasmic organelles in muscles of mice deficient in α-dystrobrevin, a component of the dystrophin-glycoprotein complex.
    Malik SO, Wierenga A, Gao C, Akaaboune M.

    06/30/2024
    alpha-Dystrobrevin knockout mice have increased motivation for appetitive reward and altered brain cannabinoid receptor 1 expression.

    α-Dystrobrevin knockout mice have increased motivation for appetitive reward and altered brain cannabinoid receptor 1 expression.
    Hawkes CA, Heath CJ, Sharp MM, Górecki DC, Carare RO., Free PMC Article

    09/24/2022
    Dystrobrevin alpha gene is a direct target of the vitamin D receptor in muscle.

    Dystrobrevin alpha gene is a direct target of the vitamin D receptor in muscle.
    Tsoumpra MK, Sawatsubashi S, Imamura M, Fukumoto S, Takeda S, Matsumoto T, Aoki Y.

    04/13/2021
    Phosphorylation of alpha-dystrobrevin is essential for alphakap accumulation and acetylcholine receptor stability.

    Phosphorylation of α-dystrobrevin is essential for αkap accumulation and acetylcholine receptor stability.
    Chen PJ, Zelada D, Belhasan DC, Akaaboune M., Free PMC Article

    01/16/2021
    these results demonstrated that, by inhibiting the activity of DTNA-mediated Notch1 axis, miR-374 could protect against myocardial I/R injury in mice after thoracic epidural anesthesia

    Protective role of microRNA-374 against myocardial ischemia-reperfusion injury in mice following thoracic epidural anesthesia by downregulating dystrobrevin alpha-mediated Notch1 axis.
    Zhao Z, Zhao Y, Ying-Chun L, Zhao L, Zhang W, Yang JG.

    05/16/2020
    A phosphorylation site on alpha-dystrobrevin-1 is essential for functional interactions with several proteins at the neuromuscular junction.

    Α-Dystrobrevin-1 recruits Grb2 and α-catulin to organize neurotransmitter receptors at the neuromuscular junction.
    Gingras J, Gawor M, Bernadzki KM, Grady RM, Hallock P, Glass DJ, Sanes JR, Proszynski TJ., Free PMC Article

    12/17/2016
    Alpha-dystrobrevin is a multifunctional protein that increases dystrophin's binding to the dystrophin-glycoprotein complex.

    Dystrobrevin increases dystrophin's binding to the dystrophin-glycoprotein complex and provides protection during cardiac stress.
    Strakova J, Dean JD, Sharpe KM, Meyers TA, Odom GL, Townsend D., Free PMC Article

    10/17/2015
    Loss of alpha dystrobrevin is associated with perturbation in cell cycle progression and nuclei shape.

    Nuclear localization of the dystrophin-associated protein α-dystrobrevin through importin α2/β1 is critical for interaction with the nuclear lamina/maintenance of nuclear integrity.
    Aguilar A, Wagstaff KM, Suárez-Sánchez R, Zinker S, Jans DA, Cisneros B.

    08/1/2015
    Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology.

    Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology.
    Na I, Redmon D, Kopa M, Qin Y, Xue B, Uversky VN., Free PMC Article

    04/5/2014
    alpha-dystrobrevin emerges as a central organizer of dystrophin-associated protein in glial endfeet and a rare example of a glial protein with a role in maintaining BBB function

    Absence of glial α-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema.
    Lien CF, Mohanta SK, Frontczak-Baniewicz M, Swinny JD, Zablocka B, Górecki DC., Free PMC Article

    02/9/2013
    the interaction between alpha-catulin and alpha-dystrobrevin is evolutionarily conserved in C. elegans and mouse muscles and strongly suggests that this interaction contributes to the integrity of the dystrophin complex

    Interaction of α-catulin with dystrobrevin contributes to integrity of dystrophin complex in muscle.
    Oh HJ, Abraham LS, van Hengel J, Stove C, Proszynski TJ, Gevaert K, DiMario JX, Sanes JR, van Roy F, Kim H., Free PMC Article

    09/22/2012
    The ErbB2 signaling maintains high efficacy of synaptic transmission by stabilizing the postsynaptic apparatus via phosphorylation of alpha-dystrobrevin1.

    Neuregulin/ErbB regulate neuromuscular junction development by phosphorylation of α-dystrobrevin.
    Schmidt N, Akaaboune M, Gajendran N, Martinez-Pena y Valenzuela I, Wakefield S, Thurnheer R, Brenner HR., Free PMC Article

    02/18/2012
    This is the first demonstration in which assembly of an astroglial protein scaffold containing syntrophin and dystrophin in perivascular astrocytes is dependent on the presence of alpha-dystrobrevin.

    Dystrophin-associated protein scaffolding in brain requires alpha-dystrobrevin.
    Bragg AD, Das SS, Froehner SC., Free PMC Article

    10/23/2010
    Fundamental functional differences between the alpha-dystrobrevins of mice and humans raises questions about the use of the mouse as a model animal for Duchenne muscular dystrophy.

    Profound human/mouse differences in alpha-dystrobrevin isoforms: a novel syntrophin-binding site and promoter missing in mouse and rat.
    Böhm SV, Constantinou P, Tan S, Jin H, Roberts RG., Free PMC Article

    01/21/2010
    This study suggests that alpha dystrobrevin is a significant component of the muscle intrinsic program that mediates the formation of complex AChR aggregates.

    Formation of complex AChR aggregates in vitro requires alpha-dystrobrevin.
    Pawlikowski BT, Maimone MM.

    01/21/2010
    Mice deficient for alpha-dystrobrevin (adbn(-/-)) exhibit extensive myofiber degeneration and neuromuscular junction abnormalities

    Destabilization of the dystrophin-glycoprotein complex without functional deficits in alpha-dystrobrevin null muscle.
    Bunnell TM, Jaeger MA, Fitzsimons DP, Prins KW, Ervasti JM., Free PMC Article

    01/21/2010
    We propose that alpha-DB plays a role in a structure or regulation mechanism unique to MCH-expressing neurons.

    Synaptic alpha-dystrobrevin: localization of a short alpha-dystrobrevin isoform in melanin-concentrating hormone neurons of the hypothalamus.
    Hazai D, Lien CF, Hajós F, Halasy K, Górecki DC, Jancsik V.

    01/21/2010
    Expression of palmitoylated alpha-dystrobrevin prevented the muscular dystrophy observed in the alpha-dystrobrevin-null mice, demonstrating that the altered form of alpha-dystrobrevin was functional.

    Differential targeting of nNOS and AQP4 to dystrophin-deficient sarcolemma by membrane-directed alpha-dystrobrevin.
    Adams ME, Tesch Y, Percival JM, Albrecht DE, Conhaim JI, Anderson K, Froehner SC.

    01/21/2010
    Complete deletion of Dtna isoforms does not reveal any new neuromuscular junction phenotype.

    Complete deletion of all alpha-dystrobrevin isoforms does not reveal new neuromuscular junction phenotype.
    Wang D, Kelly BB, Albrecht DE, Adams ME, Froehner SC, Feng G., Free PMC Article

    01/21/2010
    identified a new dystrobrevin-associated protein, DAMAGE; interacts with the N-terminal region of alpha-dystrobrevin

    DAMAGE, a novel alpha-dystrobrevin-associated MAGE protein in dystrophin complexes.
    Albrecht DE, Froehner SC.

    01/21/2010
    kinetics of the dystrobrevin-Kif5A interaction showed a lower affinity of alpha compared to that of beta-dystrobrevin for binding to kinesin

    Molecular basis of dystrobrevin interaction with kinesin heavy chain: structural determinants of their binding.
    Ceccarini M, Torreri P, Lombardi DG, Macchia G, Macioce P, Petrucci TC.

    01/21/2010
    AlphaDB, betaDB, & dystrophin are concentrated at a discrete subset of inhibitory synapses on the somata & dendrites of cerebellar Purkinje cells. Sensorimotor behaviors reflecting cerebellar function are perturbed in mice lacking any of these proteins.

    Cerebellar synaptic defects and abnormal motor behavior in mice lacking alpha- and beta-dystrobrevin.
    Grady RM, Wozniak DF, Ohlemiller KK, Sanes JR., Free PMC Article

    01/21/2010
    biglycan is important for the maintenance of muscle cell integrity and plays a direct role in regulating the expression and sarcolemmal localization of the intracellular signaling proteins dystrobrevin-1 and -2, alpha- and beta1-syntrophin and nNOS

    Biglycan regulates the expression and sarcolemmal localization of dystrobrevin, syntrophin, and nNOS.
    Mercado ML, Amenta AR, Hagiwara H, Rafii MS, Lechner BE, Owens RT, McQuillan DJ, Froehner SC, Fallon JR., Free PMC Article

    01/21/2010
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