Promotion and suppression of centriole duplication are catalytically coupled through PLK4 to ensure centriole homeostasis Journal Article

   

Authors:	Kim, M.; O'Rourke, B. P.; Soni, R. K.; Jallepalli, P. V.; Hendrickson, R. C.; Tsou, M. F. B.
Article Title:	Promotion and suppression of centriole duplication are catalytically coupled through PLK4 to ensure centriole homeostasis
Abstract:	PLK4 is the major kinase driving centriole duplication. Duplication occurs only once per cell cycle, forming one new (or daughter) centriole that is tightly engaged to the preexisting (or mother) centriole. Centriole engagement is known to block the reduplication of mother centrioles, but the molecular identity responsible for the block remains unclear. Here, we show that the centriolar cartwheel, the geometric scaffold for centriole assembly, forms the identity of daughter centrioles essential for the block, ceasing further duplication of the mother centriole to which it is engaged. To ensure a steady block, we found that the cartwheel requires constant maintenance by PLK4 through phosphorylation of the same substrate that drives centriole assembly, revealing a parsimonious control in which “assembly” and “block for new assembly” are linked through the same catalytic reaction to achieve homeostasis. Our results support a recently deduced model that the cartwheel-bound PLK4 directly suppresses centriole reduplication. © 2016 The Author(s)
Keywords:	signal transduction; controlled study; nonhuman; animal cell; enzyme activity; enzyme phosphorylation; catalysis; metabolic inhibition; cellular parameters; priority journal; article; centriole duplication; centriole homeostasis; polo like kinase 4; centriole assembly; organelle biogenesis
Journal Title:	Cell Reports
Volume:	16
Issue:	5
ISSN:	2211-1247
Publisher:	Cell Press
Date Published:	2016-08-02
Start Page:	1195
End Page:	1203
Language:	English
DOI:	10.1016/j.celrep.2016.06.069
PROVIDER:	scopus
PMCID:	PMC4972634
PUBMED:	27425613
DOI/URL:	https://www.scopus.com/inward/record.uri?eid=2-s2.0-84978827216&partnerID=40&md5=26ce66290782188e7e7ef6e35893261d
Notes:	Article -- Export Date: 1 November 2016 -- Source: Scopus

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