ArticleNature structural & molecular biology2014
Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis.
Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
72 citing papers in PubMed, 113 citations in OpenAlex.
- Article
- Genetic alterations in SUPT6H are associated with neurodevelopmental disorders.Biochimica et biophysica acta. Molecular basis of disease · 2026Article
- Distinct pathophysiological mechanisms of CEP152 variants in microcephaly and brain abnormalities.EMBO molecular medicine · 2026Article
- Article
- Critical constituents and assembly principles of centriole biogenesis in human cells.Nature reviews. Molecular cell biology · 2026Review
- NuSAP Safeguards Centriole Integrity to Mediate CEP57-CEP152 Torus Recruitment for Proper Engagement.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- PLK4: Master Regulator of Centriole Duplication and Its Therapeutic Potential.Cytoskeleton (Hoboken, N.J.) · 2025Review
- Treatment of glioblastoma with tumor-specific amplitude-modulated radiofrequency electromagnetic fields.Oncotarget · 2025Article
- Binding of CEP152 to PLK4 stimulates kinase activity to promote centriole assembly.Molecular biology of the cell · 2025Article
- Meiotic divisions and round spermatid formation do not require centriole duplication in mice.PLoS genetics · 2025Article
- CRL4Life science alliance · 2024Article
- Non-random spatial organization of telomeres varies during the cell cycle and requires LAP2 and BAF.iScience · 2024Article
- Centrosome amplification and aneuploidy driven by the HIV-1-induced Vpr•VprBP•Plk4 complex in CD4Nature communications · 2024Article
- PLK4 self-phosphorylation drives the selection of a single site for procentriole assembly.The Journal of cell biology · 2023Article
- Centrosomal organization of Cep152 provides flexibility in Plk4 and procentriole positioning.The Journal of cell biology · 2023Article
- A simple Turing reaction-diffusion model explains how PLK4 breaks symmetry during centriole duplication and assembly.PLoS biology · 2023Article
- Architectural basis for cylindrical self-assembly governing Plk4-mediated centriole duplication in human cells.Communications biology · 2023Article
- Polo-like kinase 4 homodimerization and condensate formation regulate its own protein levels but are not required for centriole assembly.Molecular biology of the cell · 2023Article
- In Search of a Mechanistic Link between Chlamydia trachomatis-Induced Cellular Pathophysiology and Oncogenesis.Infection and immunity · 2023Review
- A catalog of numerical centrosome defects in epithelial ovarian cancers.EMBO molecular medicine · 2022Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
20 authors at 10 institutions in 3 countries.
Funding
Abstract
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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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.