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  Polo-like kinase phosphorylation determines Caenorhabditis elegans centrosome size and density by biasing SPD-5 toward an assembly-competent conformation

Wueseke, O., Zwicker, D., Schwager, A., Wong, Y. L., Oegema, K., Jülicher, F., et al. (2016). Polo-like kinase phosphorylation determines Caenorhabditis elegans centrosome size and density by biasing SPD-5 toward an assembly-competent conformation. Biology Open, 5(10), 1431-1440. doi:10.1242/bio.020990.

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http://bio.biologists.org/content/5/10/1431 (Verlagsversion)
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 Urheber:
Wueseke, Oliver1, Autor
Zwicker, David1, Autor
Schwager, Anne1, Autor
Wong, Yao Liang1, Autor
Oegema, Karen1, Autor
Jülicher, Frank2, Autor           
Hyman, Anthony A.1, Autor
Woodruff, Jeffrey B.1, Autor
Affiliations:
1external, ou_persistent22              
2Max Planck Institute for the Physics of Complex Systems, Max Planck Society, ou_2117288              

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 MPIPKS: Living matter
 Zusammenfassung: Centrosomes are major microtubule-organizing centers composed of centrioles surrounded by an extensive proteinacious layer called the pericentriolar material (PCM). In Caenorhabditis elegans embryos, the mitotic PCM expands by Polo-like kinase 1 (PLK-1) phosphorylation-accelerated assembly of SPD-5 molecules into supramolecular scaffolds. However, how PLK-1 phosphorylation regulates SPD-5 assembly is not known. We found that a mutant version of SPD-5 that is insensitive to PLK-1 phosphorylation (SPD-5(4A)) could localize to PCM but was unable to rescue the reduction in PCM size and density when wild-type SPD-5 levels were decreased. In vitro, purified SPD-54A self-assembled into functional supramolecular scaffolds over long time scales, suggesting that phosphorylation only controls the rate of SPD-5 scaffold assembly. Furthermore, the SPD-5 scaffold, once assembled, remained intact and supported microtubule nucleation in the absence of PLK-1 activity in vivo. We conclude that PLK-1 is required for rapid assembly of the PCM scaffold but not for scaffold maintenance or function. Based on this idea, we developed a theoretical model that adequately predicted PCM growth rates in different mutant conditions in vivo. We propose that PLK-1 phosphorylation-dependent conversion of SPD-5 into an assembly-competent form underlies PCM formation in vivo and that the rate of this conversion determines final PCM size and density.

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 Datum: 2016-10-15
 Publikationsstatus: Erschienen
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 Identifikatoren: DOI: 10.1242/bio.020990
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Titel: Biology Open
Genre der Quelle: Zeitschrift
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Seiten: - Band / Heft: 5 (10) Artikelnummer: - Start- / Endseite: 1431 - 1440 Identifikator: -