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    The XMAP215 homologue Stu2 at yeast spindle pole bodies regulates microtubule dynamics and anchorage.

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    Authors
    Usui, Takeo
    Maekawa, Hiromi
    Pereira, Gislene
    Schiebel, Elmar
    Affiliation
    The Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Wilmslow Road, Manchester M20 4BX, UK.
    Issue Date
    2003-09-15
    
    Metadata
    Show full item record
    Abstract
    The yeast protein Stu2 belongs to the XMAP215 family of conserved microtubule-binding proteins which regulate microtubule plus end dynamics. XMAP215-related proteins also bind to centrosomes and spindle pole bodies (SPBs) through proteins like the mammalian transforming acidic coiled coil protein TACC or the yeast Spc72. We show that yeast Spc72 has two distinct domains involved in microtubule organization. The essential 100 N-terminal amino acids of Spc72 interact directly with the gamma-tubulin complex, and an adjacent non-essential domain of Spc72 mediates binding to Stu2. Through these domains, Spc72 brings Stu2 and the gamma-tubulin complex together into a single complex. Manipulation of Spc72-Stu2 interaction at SPBs compromises the anchorage of astral microtubules at the SPB and surprisingly also influences the dynamics of microtubule plus ends. Permanently tethering Stu2 to SPBs by fusing it to a version of Spc72 that lacks the Stu2-binding site in part complements these defects in a manner which is dependent upon the microtubule-binding domain of Stu2. Thus, the SPB-associated Spc72-Stu2 complex plays a key role in regulating microtubule properties.
    Citation
    The XMAP215 homologue Stu2 at yeast spindle pole bodies regulates microtubule dynamics and anchorage. 2003, 22 (18):4779-93 EMBO J.
    Journal
    The EMBO Journal
    URI
    http://hdl.handle.net/10541/82123
    DOI
    10.1093/emboj/cdg459
    PubMed ID
    12970190
    Type
    Article
    Language
    en
    ISSN
    0261-4189
    ae974a485f413a2113503eed53cd6c53
    10.1093/emboj/cdg459
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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