An ordered pattern of Ana2 phosphorylation by Plk4 is required for centriole assembly
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.
Affiliation
Univ Arizona, Canc Ctr, Dept Cellular & Mol MedIssue Date
2018-03-01
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ROCKEFELLER UNIV PRESSCitation
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.201605106Journal
JOURNAL OF CELL BIOLOGYRights
© 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 2018ISSN
0021-95251540-8140
PubMed ID
29496738Version
Final published versionSponsors
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 FriendsAdditional Links
http://www.jcb.org/lookup/doi/10.1083/jcb.201605106ae974a485f413a2113503eed53cd6c53
10.1083/jcb.201605106
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