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dc.contributor.authorMcLamarrah, Tiffany A.
dc.contributor.authorBuster, Daniel W.
dc.contributor.authorGalletta, Brian J.
dc.contributor.authorBoese, Cody J.
dc.contributor.authorRyniawec, John M.
dc.contributor.authorHollingsworth, Natalie Ann
dc.contributor.authorByrnes, Amy E.
dc.contributor.authorBrownlee, Christopher W.
dc.contributor.authorSlep, Kevin C.
dc.contributor.authorRusan, Nasser M.
dc.contributor.authorRogers, Gregory C.
dc.date.accessioned2018-05-14T22:52:02Z
dc.date.available2018-05-14T22:52:02Z
dc.date.issued2018-03-01
dc.identifier.citationAn 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.201605106en_US
dc.identifier.issn0021-9525
dc.identifier.issn1540-8140
dc.identifier.pmid29496738
dc.identifier.doi10.1083/jcb.201605106
dc.identifier.urihttp://hdl.handle.net/10150/627615
dc.description.abstractPolo-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.en_US
dc.description.sponsorshipDivision 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 Friendsen_US
dc.language.isoenen_US
dc.publisherROCKEFELLER UNIV PRESSen_US
dc.relation.urlhttp://www.jcb.org/lookup/doi/10.1083/jcb.201605106en_US
dc.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.en_US
dc.rights.urihttps://creativecommons.org/licenses/by-nc-sa/4.0/
dc.titleAn ordered pattern of Ana2 phosphorylation by Plk4 is required for centriole assemblyen_US
dc.typeArticleen_US
dc.contributor.departmentUniv Arizona, Canc Ctr, Dept Cellular & Mol Meden_US
dc.identifier.journalJOURNAL OF CELL BIOLOGYen_US
dc.description.note6 month embargo; published online: 1 March 2018en_US
dc.description.collectioninformationThis 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.en_US
dc.eprint.versionFinal published versionen_US
dc.source.journaltitleThe Journal of Cell Biology
dc.source.volume217
dc.source.issue4
dc.source.beginpage1217
dc.source.endpage1231


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© 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.
Except where otherwise noted, this item's license is described as © 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.