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2016 ; 17
(3
): 326-37
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A non-canonical function of Plk4 in centriolar satellite integrity and
ciliogenesis through PCM1 phosphorylation
#MMPMID26755742
Hori A
; Barnouin K
; Snijders AP
; Toda T
EMBO Rep
2016[Mar]; 17
(3
): 326-37
PMID26755742
show ga
Centrioles are the major constituents of the animal centrosome, in which Plk4
kinase serves as a master regulator of the duplication cycle. Many eukaryotes
also contain numerous peripheral particles known as centriolar satellites. While
centriolar satellites aid centriole assembly and primary cilium formation, it is
unknown whether Plk4 plays any regulatory roles in centriolar satellite
integrity. Here we show that Plk4 is a critical determinant of centriolar
satellite organisation. Plk4 depletion leads to the dispersion of centriolar
satellites and perturbed ciliogenesis. Plk4 interacts with the satellite
component PCM1, and its kinase activity is required for phosphorylation of the
conserved S372. The nonphosphorylatable PCM1 mutant recapitulates phenotypes of
Plk4 depletion, while the phosphomimetic mutant partially rescues the dispersed
centriolar satellite patterns and ciliogenesis in cells depleted of PCM1. We show
that S372 phosphorylation occurs during the G1 phase of the cell cycle and is
important for PCM1 dimerisation and interaction with other satellite components.
Our findings reveal that Plk4 is required for centriolar satellite function,
which may underlie the ciliogenesis defects caused by Plk4 dysfunction.