Number of the records: 1  

TPX2 Protein of Arabidopsis Activates Aurora Kinase 1, But Not Aurora Kinase 3 In Vitro

  1. 1.
    SYSNO ASEP0454970
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleTPX2 Protein of Arabidopsis Activates Aurora Kinase 1, But Not Aurora Kinase 3 In Vitro
    Author(s) Tomaštíková, Eva (UEB-Q) RID, ORCID
    Demidov, D. (DE)
    Jeřábková, Hana (UEB-Q) RID, ORCID
    Binarová, Pavla (MBU-M) RID, ORCID
    Houben, A. (DE)
    Doležel, Jaroslav (UEB-Q) RID, ORCID
    Petrovská, Beáta (UEB-Q) RID, ORCID
    Source TitlePlant Molecular Biology Reporter - ISSN 0735-9640
    Roč. 33, č. 6 (2015), s. 1988-1995
    Number of pages8 s.
    Languageeng - English
    CountryUS - United States
    KeywordsAurora kinase ; Targeting protein for Xklp2 ; In vitro kinase assay
    Subject RIVEB - Genetics ; Molecular Biology
    R&D ProjectsGA14-28443S GA ČR - Czech Science Foundation (CSF)
    LO1204 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    GAP501/12/2333 GA ČR - Czech Science Foundation (CSF)
    Institutional supportUEB-Q - RVO:61389030 ; MBU-M - RVO:61388971
    UT WOS000367464000031
    DOI10.1007/s11105-015-0890-x
    AnnotationAurora kinases are involved in various mitotic events, including chromosome segregation and bipolar mitotic spindle assembly. In animals, Aurora A is activated and protected by microtubule-associated protein TPX2. Such role in plants is not known. Here, we have assessed the ability of TPX2 of Arabidopsis to regulate Aurora family members in vitro. AtTPX2 acts as substrate as well as activator of AtAurora1, but not AtAurora3. Truncated version of AtTPX2 lacking the Aurora binding domain is unable to activate the kinases; however, it is still phosphorylated. AtTPX2-induced activation of AtAurora1 results in a dramatically increased phosphorylation level of downstream targets, particularly histone H3. The differences in the activation mechanism of AtAurora1 and 3 point to a specific regulation of both kinases, which may play an important role in cell cycle regulation and signaling cascade transduction in plants.
    WorkplaceInstitute of Experimental Botany
    ContactDavid Klier, knihovna@ueb.cas.cz, Tel.: 220 390 469
    Year of Publishing2016
Number of the records: 1  

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