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- 저자 : Cheary, Donna-Marie (검색결과 1 건)
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Multisite phosphorylation of C-Nap1 releases it from Cep135 to trigger centrosome disjunction
Hardy, Tara,Lee, Miseon,Hames, Rebecca S.,Prosser, Suzanna L.,Cheary, Donna-Marie,Samant, Mugdha D.,Schultz, Francisca,Baxter, Joanne E.,Rhee, Kunsoo,Fry, Andrew M. The Company of Biologists 2014 Journal of cell science Vol.127 No.11
<P><B>ABSTRACT</B></P><P>During mitotic entry, centrosomes separate to establish the bipolar spindle. Delays in centrosome separation can perturb chromosome segregation and promote genetic instability. However, interphase centrosomes are physically tethered by a proteinaceous linker composed of C-Nap1 (also known as CEP250) and the filamentous protein rootletin. Linker disassembly occurs at the onset of mitosis in a process known as centrosome disjunction and is triggered by the Nek2-dependent phosphorylation of C-Nap1. However, the mechanistic consequences of C-Nap1 phosphorylation are unknown. Here, we demonstrate that Nek2 phosphorylates multiple residues within the C-terminal domain of C-Nap1 and, collectively, these phosphorylation events lead to loss of oligomerization and centrosome association. Mutations in non-phosphorylatable residues that make the domain more acidic are sufficient to release C-Nap1 from the centrosome, suggesting that it is an increase in overall negative charge that is required for this process. Importantly, phosphorylation of C-Nap1 also perturbs interaction with the core centriolar protein, Cep135, and interaction of endogenous C-Nap1 and Cep135 proteins is specifically lost in mitosis. We therefore propose that multisite phosphorylation of C-Nap1 by Nek2 perturbs both oligomerization and Cep135 interaction, and this precipitates centrosome disjunction at the onset of mitosis.</P>
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