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    STU2 Stu2p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 850734, updated on 9-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    The TOG protein Stu2 is regulated by acetylation.

    The TOG protein Stu2 is regulated by acetylation.
    Greenlee MA, Witt B, Sabo JA, Morris SC, Miller RK., Free PMC Article

    10/8/2022
    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
    Study identifies a Stu2 mutant that abolishes its kinetochore function and shows that it causes biorientation defects in vivo. Stu2-mediated pathway functions together with the Aurora B-mediated pathway. Altogether, work indicates that cells employ multiple pathways to ensure biorientation and the accuracy of chromosome segregation.

    Kinetochore-associated Stu2 promotes chromosome biorientation in vivo.
    Miller MP, Evans RK, Zelter A, Geyer EA, MacCoss MJ, Rice LM, Davis TN, Asbury CL, Biggins S., Free PMC Article

    02/15/2020
    Findings raise the possibility that the microtubule polymerization activities mediated by Stu2p are regulated through sumoylation pathways.

    The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO.
    Greenlee M, Alonso A, Rahman M, Meednu N, Davis K, Tabb V, Cook R, Miller RK., Free PMC Article

    10/26/2019
    An unexpected antagonism has been found between the tubulin-binding Stu2 domains (TOGs) and the lattice-binding basic region: lattice binding by the basic region is weak when at least two TOGs engage tubulins, strong when TOGs are empty.

    Design principles of a microtubule polymerase.
    Geyer EA, Miller MP, Brautigam CA, Biggins S, Rice LM., Free PMC Article

    04/20/2019
    TORC1/Kog1 signaling controls Stu2 localization and thereby contributes to proper microtubule cytoskeletal organization in interphase and mitosis.

    TORC1 signaling exerts spatial control over microtubule dynamics by promoting nuclear export of Stu2.
    van der Vaart B, Fischböck J, Mieck C, Pichler P, Mechtler K, Medema RH, Westermann S., Free PMC Article

    11/25/2017
    findings reveal an uncharacterized function of Stu2 that is regulated mechanically, such that kinetochore-microtubule attachments are intrinsically stabilized by tension, implicating it in the correction of erroneous kinetochore-microtubule attachments

    A TOG Protein Confers Tension Sensitivity to Kinetochore-Microtubule Attachments.
    Miller MP, Asbury CL, Biggins S., Free PMC Article

    12/17/2016
    Stu2p/XMAP215 proteins are essential microtubule polymerases that use multiple alpha-beta-tubulin-interacting TOG domains to bind microtubule plus ends and catalyze fast microtubule growth.

    A tethered delivery mechanism explains the catalytic action of a microtubule polymerase.
    Ayaz P, Munyoki S, Geyer EA, Piedra FA, Vu ES, Bromberg R, Otwinowski Z, Grishin NV, Brautigam CA, Rice LM., Free PMC Article

    05/16/2015
    Stu2 is a Saccharomyces cerevisiae microtubule polymerase.

    Stu2, the budding yeast XMAP215/Dis1 homolog, promotes assembly of yeast microtubules by increasing growth rate and decreasing catastrophe frequency.
    Podolski M, Mahamdeh M, Howard J., Free PMC Article

    02/7/2015
    anaphase Stu2-dependent microtubule dynamics are critical for separation of long chromosomes.

    Chromosome length and perinuclear attachment constrain resolution of DNA intertwines.
    Titos I, Ivanova T, Mendoza M., Free PMC Article

    11/22/2014
    The microtubule rescue distal to the kinetochore is also promoted by Stu2, which is transported by a kinesin-8 motor Kip3 along the microtubule from the kinetochore.

    Kinetochore-dependent microtubule rescue ensures their efficient and sustained interactions in early mitosis.
    Gandhi SR, Gierliński M, Mino A, Tanaka K, Kitamura E, Clayton L, Tanaka TU., Free PMC Article

    02/4/2012
    Crystal structures of the tubulin binding domains of XMAP215 (yeast Stu2p and Drosophila Msps), EB1 (yeast Bim1p and human EB1), and CLIP-170 (human), which reveal diverse tubulin binding interfaces, are reported.

    Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1.
    Slep KC, Vale RD., Free PMC Article

    01/21/2010
    Mislocalization of Stu2 results in premature spindle expansion in S phase stalled spc24-9 mutants.

    Spc24 and Stu2 promote spindle integrity when DNA replication is stalled.
    Ma L, McQueen J, Cuschieri L, Vogel J, Measday V., Free PMC Article

    01/21/2010
    Stu2p binds to a single free tubulin heterodimer through its first TOG domain and has the capacity to associate directly with microtubule ends, at least in part, through its second TOG domain.

    Stu2p binds tubulin and undergoes an open-to-closed conformational change.
    Al-Bassam J, van Breugel M, Harrison SC, Hyman A., Free PMC Article

    01/21/2010
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