Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 21, Issue 8, Pages 696-703Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2846
Keywords
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Funding
- intramural research grants of the US National Cancer Institute
- National Institute of Diabetes and Digestive and Kidney Diseases
- National Research Foundation of Korea (NRF) Global Research Laboratory program [K20815000001]
- NRF [2011-0030027]
- NRF National Leap Research Program [2010-0029233]
- Global Frontier Project [NRF-M1AXA002-2012M3A6A4054949]
- Korea Basic Science Institute [T33418]
- World Class Institute program grant - Ministry of Science, ICT and Future Planning of the Republic of Korea [2009-002]
- Next-Generation BioGreen 21 Program from the Rural Development Administration, Republic of Korea [PJ009594]
- Ministry of Education, Sports, Science and Technology of Japan [23380065]
- Grants-in-Aid for Scientific Research [23380065] Funding Source: KAKEN
- Korea Evaluation Institute of Industrial Technology (KEIT) [2009-002] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [2010-0029233] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Polo-like kinase 4 (Plk4) is a key regulator of centriole duplication, an event critical for the maintenance of genomic integrity. We show that Plk4 relocalizes from the inner Cep192 ring to the outer Cep152 ring as newly recruited Cep152 assembles around the Cep192-encircled daughter centriole. Crystal-structure analyses revealed that Cep192- and Cep152-derived peptides bind the cryptic polo box (CPB) of Plk4 in opposite orientations and in a mutually exclusive manner. The Cep152 peptide bound to the CPB markedly better than did the Cep192 peptide and effectively 'snatched' the CPB away from a preformed CPB Cep192 peptide complex. A cancer-associated Cep152 mutation impairing the Plk4 interaction induced defects in procentriole assembly and chromosome segregation. Thus, Plk4 is intricately regulated in time and space through ordered interactions with two distinct scaffolds, Cep192 and Cep152, and a failure in this process may lead to human cancer.
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