An ordered pattern of Ana2 phosphorylation by Plk4 is required for centriole assembly.
J Cell Biol
; 217(4): 1217-1231, 2018 04 02.
Article
em En
| MEDLINE
| ID: mdl-29496738
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.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Ciclo Celular
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Centríolos
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Proteínas Serina-Treonina Quinases
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Proteínas de Ciclo Celular
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Proteínas de Drosophila
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Drosophila melanogaster
Limite:
Animals
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article