An ordered pattern of Ana2 phosphorylation by Plk4 is required for centriole assembly
AuthorMcLamarrah, 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.
AffiliationUniv Arizona, Canc Ctr, Dept Cellular & Mol Med
MetadataShow full item record
PublisherROCKEFELLER UNIV PRESS
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.201605106
JournalJOURNAL OF CELL BIOLOGY
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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.
Note6 month embargo; published online: 1 March 2018
VersionFinal published version
SponsorsDivision 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
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