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    An ordered pattern of Ana2 phosphorylation by Plk4 is required for centriole assembly

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    Author
    McLamarrah, Tiffany A.
    Buster, Daniel W.
    Galletta, Brian J.
    Boese, Cody J.
    Ryniawec, John M.
    Hollingsworth, Natalie Ann
    Byrnes, Amy E.
    Brownlee, Christopher W.
    Slep, Kevin C.
    Rusan, Nasser M.
    Rogers, Gregory C.
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    Affiliation
    Univ Arizona, Canc Ctr, Dept Cellular & Mol Med
    Issue Date
    2018-03-01
    
    Metadata
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    Publisher
    ROCKEFELLER UNIV PRESS
    Citation
    An ordered pattern of Ana2 phosphorylation by Plk4 is required for centriole assembly Tiffany A. McLamarrah, Daniel W. Buster, Brian J. Galletta, Cody J. Boese, John M. Ryniawec, Natalie Ann Hollingsworth, Amy E. Byrnes, Christopher W. Brownlee, Kevin C. Slep, Nasser M. Rusan, Gregory C. Rogers J Cell Biol Apr 2018, 217 (4) 1217-1231; DOI: 10.1083/jcb.201605106
    Journal
    JOURNAL OF CELL BIOLOGY
    Rights
    © 2018 McLamarrah et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license.
    Collection Information
    This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.
    Abstract
    Polo-like kinase 4 (Plk4) initiates an early step in centriole assembly by phosphorylating Ana2/STIL, a structural component of the procentriole. Here, we show that Plk4 binding to the central coiled-coil (CC) of Ana2 is a conserved event involving Polo-box 3 and a previously unidentified putative CC located adjacent to the kinase domain. Ana2 is then phosphorylated along its length. Previous studies showed that Plk4 phosphorylates the C-terminal STil/ANa2 (STAN) domain of Ana2/STIL, triggering binding and recruitment of the cartwheel protein Sas6 to the procentriole assembly site. However, the physiological relevance of N-terminal phosphorylation was unknown. We found that Plk4 first phosphorylates the extreme N terminus of Ana2, which is critical for subsequent STAN domain modification. Phosphorylation of the central region then breaks the Plk4-Ana2 interaction. This phosphorylation pattern is important for centriole assembly and integrity because replacement of endogenous Ana2 with phospho-Ana2 mutants disrupts distinct steps in Ana2 function and inhibits centriole duplication.
    Note
    6 month embargo; published online: 1 March 2018
    ISSN
    0021-9525
    1540-8140
    PubMed ID
    29496738
    DOI
    10.1083/jcb.201605106
    Version
    Final published version
    Sponsors
    Division of Intramural Research at the National Heart, Lung, and Blood Institute [1ZIA HL006104]; National Cancer Institute [P30 CA23074]; National Institute of General Medical Sciences [R01GFM110166]; National Science Foundation [MCB1158151]; Phoenix Friends
    Additional Links
    http://www.jcb.org/lookup/doi/10.1083/jcb.201605106
    ae974a485f413a2113503eed53cd6c53
    10.1083/jcb.201605106
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