• Login
    View Item 
    •   Maryland Shared Open Access Repository Home
    • ScholarWorks@UMBC
    • UMBC College of Natural and Mathematical Sciences
    • UMBC Biological Sciences Department
    • View Item
    •   Maryland Shared Open Access Repository Home
    • ScholarWorks@UMBC
    • UMBC College of Natural and Mathematical Sciences
    • UMBC Biological Sciences Department
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p

    Thumbnail
    Links to Files
    https://www.cell.com/cell/fulltext/S0092-8674(02)00973-X?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS009286740200973X%3Fshowall%3Dtrue
    Permanent Link
    https://doi.org/10.1016/S0092-8674(02)00973-X
    http://hdl.handle.net/11603/26705
    Collections
    • UMBC Biological Sciences Department
    Metadata
    Show full item record
    Author/Creator
    Cheeseman, Iain M
    Anderson, Scott
    Jwa, Miri
    Green, Erin
    Kang, Jung seog
    3rd, John R Yates
    Chan, Clarence S M
    Drubin, David G
    Barnes, Georjana
    Author/Creator ORCID
    https://orcid.org/0000-0003-3923-6726
    Date
    2002-10-18
    Type of Work
    10 pages
    Text
    journal articles
    Citation of Original Publication
    Cheeseman, Iain M et al. “Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p.” Cell vol. 111,2 (2002): 163-72. doi:10.1016/s0092-8674(02)00973-x
    Rights
    This item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.
    Subjects
    kinetochore-microtubule
    Ipl1p
    Abstract
    The Aurora kinase Ipl1p plays a crucial role in regulating kinetochore-microtubule attachments in budding yeast, but the underlying basis for this regulation is not known. To identify Ipl1p targets, we first purified 28 kinetochore proteins from yeast protein extracts. These studies identified five previously uncharacterized kinetochore proteins and defined two additional kinetochore subcomplexes. We then used mass spectrometry to identify 18 phosphorylation sites in 7 of these 28 proteins. Ten of these phosphorylation sites are targeted directly by Ipl1p, allowing us to identify a consensus phosphorylation site for an Aurora kinase. Our systematic mutational analysis of the Ipl1p phosphorylation sites demonstrated that the essential microtubule binding protein Dam1p is a key Ipl1p target for regulating kinetochore-microtubule attachments in vivo.


    Albin O. Kuhn Library & Gallery
    University of Maryland, Baltimore County
    1000 Hilltop Circle
    Baltimore, MD 21250
    www.umbc.edu/scholarworks

    Contact information:
    Email: scholarworks-group@umbc.edu
    Phone: 410-455-3021


    If you wish to submit a copyright complaint or withdrawal request, please email mdsoar-help@umd.edu.

     

     

    My Account

    LoginRegister

    Browse

    This CollectionBy Issue DateTitlesAuthorsSubjectsType

    Statistics

    View Usage Statistics


    Albin O. Kuhn Library & Gallery
    University of Maryland, Baltimore County
    1000 Hilltop Circle
    Baltimore, MD 21250
    www.umbc.edu/scholarworks

    Contact information:
    Email: scholarworks-group@umbc.edu
    Phone: 410-455-3021


    If you wish to submit a copyright complaint or withdrawal request, please email mdsoar-help@umd.edu.