U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    Tuba1a tubulin, alpha 1A [ Mus musculus (house mouse) ]

    Gene ID: 22142, updated on 21-Apr-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    TUBA1A licenses APC/C-mediated mitotic progression to drive glioblastoma growth by inhibiting PLK3.

    TUBA1A licenses APC/C-mediated mitotic progression to drive glioblastoma growth by inhibiting PLK3.
    Wen J, Wang Q, Zhang W, Wang W.

    01/6/2024
    Codon modification of Tuba1a alters mRNA levels and causes a severe neurodevelopmental phenotype in mice.

    Codon modification of Tuba1a alters mRNA levels and causes a severe neurodevelopmental phenotype in mice.
    Leca I, Phillips AW, Ushakova L, Cushion TD, Keays DA., Free PMC Article

    03/8/2023
    A potential mechanism by which aspiration of duodenogastric fluid augments the risk for bronchiolitis obliterans syndrome after lung transplantation.

    A potential mechanism by which aspiration of duodenogastric fluid augments the risk for bronchiolitis obliterans syndrome after lung transplantation.
    Olson MT, Liu W, Mohanakumar T, Bremner RM.

    01/21/2023
    TUBA1A tubulinopathy mutants disrupt neuron morphogenesis and override XMAP215/Stu2 regulation of microtubule dynamics.

    TUBA1A tubulinopathy mutants disrupt neuron morphogenesis and override XMAP215/Stu2 regulation of microtubule dynamics.
    Hoff KJ, Aiken JE, Gutierrez MA, Franco SJ, Moore JK., Free PMC Article

    07/2/2022
    alpha-Tubulin acetylation on lysine 40 controls cardiac glucose uptake.

    α-Tubulin acetylation on lysine 40 controls cardiac glucose uptake.
    Renguet E, De Loof M, Fourny N, Ginion A, Bouzin C, Poüs C, Horman S, Beauloye C, Bultot L, Bertrand L.

    06/11/2022
    Reduced TUBA1A Tubulin Causes Defects in Trafficking and Impaired Adult Motor Behavior.

    Reduced TUBA1A Tubulin Causes Defects in Trafficking and Impaired Adult Motor Behavior.
    Buscaglia G, Northington KR, Moore JK, Bates EA., Free PMC Article

    07/31/2021
    HDAC6-mediated alpha-tubulin deacetylation suppresses autophagy and enhances motility of podocytes in diabetic nephropathy.

    HDAC6-mediated α-tubulin deacetylation suppresses autophagy and enhances motility of podocytes in diabetic nephropathy.
    Liang T, Qi C, Lai Y, Xie J, Wang H, Zhang L, Lin T, Jv M, Li J, Wang Y, Zhang Y, Chen Z, Qiu X, Li R, Li Z, Ye Z, Liu S, Liang X, Shi W, Wang W., Free PMC Article

    05/8/2021
    A proteomic survey of microtubule-associated proteins in a R402H TUBA1A mutant mouse.

    A proteomic survey of microtubule-associated proteins in a R402H TUBA1A mutant mouse.
    Leca I, Phillips AW, Hofer I, Landler L, Ushakova L, Cushion TD, Dürnberger G, Stejskal K, Mechtler K, Keays DA., Free PMC Article

    01/9/2021
    Tubulin-specific chaperon E knockdown induces the accumulation of inert alpha-tubulin that cannot form microtubules in the cell body.

    Inhibition of microtubule assembly competent tubulin synthesis leads to accumulation of phosphorylated tau in neuronal cell bodies.
    Fujiwara H, Watanabe S, Iwata M, Ueda S, Nobuhara M, Wada-Kakuda S, Misonou H, Miyasaka T.

    08/1/2020
    Study shows that loss of Tubb2a or Tubb2b does not impair survival but does lead to relatively mild cortical malformation phenotypes. In contrast, loss of Tuba1a is perinatal lethal and leads to significant forebrain dysmorphology. The ability of the mouse to survive in the absence of some tubulin genes known to cause disease in humans suggests future intervention strategies for these devastating tubulinopathy diseases.

    Differential requirements of tubulin genes in mammalian forebrain development.
    Bittermann E, Abdelhamed Z, Liegel RP, Menke C, Timms A, Beier DR, Stottmann RW., Free PMC Article

    01/11/2020
    In this study, we demonstrate that missense mutations affecting arginine at position 402 (R402) of TUBA1A alpha-tubulin selectively impair dynein motor activity and severely and dominantly disrupt cortical neuronal migration.

    TUBA1A mutations identified in lissencephaly patients dominantly disrupt neuronal migration and impair dynein activity.
    Aiken J, Moore JK, Bates EA., Free PMC Article

    07/6/2019
    Transgenic mdx mice expressing the short dystrophin isoform Dp116 served as a negative control. All mini- and micro-dystrophins restored elevated detyrosinated alpha-tubulin and microtubule density of mdx muscle to values not different from C57BL/10, however, only mini-dystrophins restored the transverse component of the microtubule lattice back to C57BL/10.

    Variable rescue of microtubule and physiological phenotypes in mdx muscle expressing different miniaturized dystrophins.
    Nelson DM, Lindsay A, Judge LM, Duan D, Chamberlain JS, Lowe DA, Ervasti JM., Free PMC Article

    03/2/2019
    Here the authors demonstrate that mice lacking the alpha-tubulin acetyltransferase Atat1 in sensory neurons display profound deficits in their ability to detect mechanical stimuli.

    Acetylated tubulin is essential for touch sensation in mice.
    Morley SJ, Qi Y, Iovino L, Andolfi L, Guo D, Kalebic N, Castaldi L, Tischer C, Portulano C, Bolasco G, Shirlekar K, Fusco CM, Asaro A, Fermani F, Sundukova M, Matti U, Reymond L, De Ninno A, Businaro L, Johnsson K, Lazzarino M, Ries J, Schwab Y, Hu J, Heppenstall PA., Free PMC Article

    11/25/2017
    Collectively, these findings suggest that Smo and primary cilia-dependent noncanonical Hh signaling leads to post-translational regulation of microtubules and may be important for modulating cell behaviors.

    Ciliary smoothened-mediated noncanonical hedgehog signaling promotes tubulin acetylation.
    Lee H, Ko HW.

    06/3/2017
    Further PS treatment resulted in recovery of axonal outgrowth and enhanced retrograde axonal transport by decreasing histone deacetylase 6 (HDAC6) levels and thus increasing acetylation of alpha-tubulin levels. Thus, we have identified the molecular pathway that leads to neurodegeneration in FD and have demonstrated that phosphatidylserine treatment has the potential to slow progression of neurodegeneration

    Phosphatidylserine Ameliorates Neurodegenerative Symptoms and Enhances Axonal Transport in a Mouse Model of Familial Dysautonomia.
    Naftelberg S, Abramovitch Z, Gluska S, Yannai S, Joshi Y, Donyo M, Ben-Yaakov K, Gradus T, Zonszain J, Farhy C, Ashery-Padan R, Perlson E, Ast G., Free PMC Article

    05/13/2017
    mass spectrometry-based quantitative comparison of acetylated peptides from wild-type vs HDAC6 knockout mice allowed to identify six new deacetylation sites possibly mediated by HDAC6.

    New HDAC6-mediated deacetylation sites of tubulin in the mouse brain identified by quantitative mass spectrometry.
    Liu N, Xiong Y, Li S, Ren Y, He Q, Gao S, Zhou J, Shui W., Free PMC Article

    09/17/2016
    These results give new insights into the functions of Tuba1a, mechanisms for regulating tubulin proteostasis, and how compromising these may lead to neural defects.

    Novel α-tubulin mutation disrupts neural development and tubulin proteostasis.
    Gartz Hanson M, Aiken J, Sietsema DV, Sept D, Bates EA, Niswander L, Moore JK., Free PMC Article

    06/28/2016
    Data indicate that alpha 1a tubulin (Tuba1a) showed the least variability in expression among the different stages of lung development.

    Validation of Tuba1a as appropriate internal control for normalization of gene expression analysis during mouse lung development.
    Mehta A, Dobersch S, Dammann RH, Bellusci S, Ilinskaya ON, Braun T, Barreto G., Free PMC Article

    01/16/2016
    Tubulin-tyrosine ligase (TTL) is required to increase the levels of tyrosinated alpha-tubulin at the axon injury site and plays an important role in injury signaling.

    Tubulin-tyrosine Ligase (TTL)-mediated Increase in Tyrosinated α-Tubulin in Injured Axons Is Required for Retrograde Injury Signaling and Axon Regeneration.
    Song W, Cho Y, Watt D, Cavalli V., Free PMC Article

    08/29/2015
    Data suggest a mechanistic link between tubulin hyperacetylation and autophagy induction.

    Tubulin hyperacetylation is adaptive in cardiac proteotoxicity by promoting autophagy.
    McLendon PM, Ferguson BS, Osinska H, Bhuiyan MS, James J, McKinsey TA, Robbins J., Free PMC Article

    05/2/2015
    TFIIB co-localizes and interacts with alpha-tubulin during oocyte meiosis in the mouse and depletion of TFIIB causes arrest of subsequent embryo development.

    TFIIB co-localizes and interacts with α-tubulin during oocyte meiosis in the mouse and depletion of TFIIB causes arrest of subsequent embryo development.
    Liu H, Yin FX, Bai CL, Shen QY, Wei ZY, Li XX, Liang H, Bou S, Li GP., Free PMC Article

    08/16/2014
    Acetylation of alpha-tubulin is under the control of the acetyltransferase MEC-17 and deacetylases SIRT2 (Sirtuin 2) and HDAC6 (histone deacetylase 6). Adipocyte development is inhibited in MEC-17-knockdown cells, but enhanced in MEC-17-overexpressing cells.

    Regulation of adipogenesis by cytoskeleton remodelling is facilitated by acetyltransferase MEC-17-dependent acetylation of α-tubulin.
    Yang W, Guo X, Thein S, Xu F, Sugii S, Baas PW, Radda GK, Han W., Free PMC Article

    03/9/2013
    Unambiguous identification of novel glutamylation sites E441 and E443 in mouse brain Tuba1a and Tuba1b.

    Analysis of tubulin alpha-1A/1B C-terminal tail post-translational poly-glutamylation reveals novel modification sites.
    Sahab ZJ, Kirilyuk A, Zhang L, Khamis ZI, Pompach P, Sung Y, Byers SW., Free PMC Article

    07/14/2012
    This study demonistrated that novel tubal(aspartic acid to glycine) mutant mouse is a novel animal model for neurodevelopmental disorders.

    Behavioral and neuromorphological characterization of a novel Tuba1 mutant mouse.
    Furuse T, Yamada I, Kushida T, Masuya H, Miura I, Kaneda H, Kobayashi K, Wada Y, Yuasa S, Wakana S.

    04/28/2012
    These results demonstrate a role for CCP1 in the processing of Glu residues from beta- as well as alpha-tubulin in vitro and in vivo.

    Cytosolic carboxypeptidase 1 is involved in processing α- and β-tubulin.
    Berezniuk I, Vu HT, Lyons PJ, Sironi JJ, Xiao H, Burd B, Setou M, Angeletti RH, Ikegami K, Fricker LD., Free PMC Article

    04/28/2012
    firstprevious page of 2 nextlast