ArticlePloS one2012
The centrosomal kinase Plk1 localizes to the transition zone of primary cilia and induces phosphorylation of nephrocystin-1.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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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
33 citing papers in PubMed, 47 citations in OpenAlex.
- Multi-omics analysis of green lineage osmotic stress pathways unveils crucial roles of different cellular compartments.Nature communications · 2024Article
- Illumination of understudied ciliary kinases.Frontiers in molecular biosciences · 2024Review
- The role of Smo-Shh/Gli signaling activation in the prevention of neurological and ageing disorders.Biogerontology · 2023Review
- The role of primary cilia in thyroid diseases.Frontiers in endocrinology · 2023Review
- LRRK1-mediated NDEL1 phosphorylation promotes cilia disassembly via dynein-2-driven retrograde intraflagellar transport.Journal of cell science · 2022Article
- Antioxidant enzyme peroxiredoxin 5 regulates cyst growth and ciliogenesis via modulating Plk1 stability.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Review
- Therapeutically actionable signaling node to rescue AURKA driven loss of primary cilia in VHL-deficient cells.Scientific reports · 2021Article
- Functional aspects of primary cilium in signaling, assembly and microenvironment in cancer.Journal of cellular physiology · 2021Review
- The Role of Primary Cilia in Thyroid Cancer: From Basic Research to Clinical Applications.Frontiers in endocrinology · 2021Review
- Article
- Phosphoproteomics of short-term hedgehog signaling in human medulloblastoma cells.Cell communication and signaling : CCS · 2020Article
- Freeing the brake: Proliferation needs primary cilium to disassemble.Journal of biosciences · 2020Review
- Restoration of primary cilia in obese adipose-derived mesenchymal stem cells by inhibiting Aurora A or extracellular signal-regulated kinase.Stem cell research & therapy · 2019Article
- HDAC3 and HDAC8 are required for cilia assembly and elongation.Biology open · 2019Article
- Cenpj Regulates Cilia Disassembly and Neurogenesis in the Developing Mouse Cortex.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019Article
- Activation of the oncogenic transcription factor B-Myb via multisite phosphorylation and prolyl cis/trans isomerization.Nucleic acids research · 2019Article
- Microscopy-Based Automated Live Cell Screening for Small Molecules That Affect Ciliation.Frontiers in genetics · 2019Article
- Strain-specific differences in brain gene expression in a hydrocephalic mouse model with motile cilia dysfunction.Scientific reports · 2018Article
- Ciliary signalling in cancer.Nature reviews. Cancer · 2018Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Polo-like kinase (Plk1) plays a central role in regulating the cell cycle. Plk1-mediated phosphorylation is essential for centrosome maturation, and for numerous mitotic events. Although Plk1 localizes to multiple subcellular sites, a major site of action is the centrosomes, which supports mitotic functions in control of bipolar spindle formation. In G0 or G1 untransformed cells, the centriolar core of the centrosome differentiates into the basal body of the primary cilium. Primary cilia are antenna-like sensory organelles dynamically regulated during the cell cycle. Whether Plk1 has a role in ciliary biology has never been studied. Nephrocystin-1 (NPHP1) is a ciliary protein; loss of NPHP1 in humans causes nephronophthisis (NPH), an autosomal-recessive cystic kidney disease. We here demonstrate that Plk1 colocalizes with nephrocystin-1 to the transition zone of primary cilia in epithelial cells. Plk1 co-immunoprecipitates with NPHP1, suggesting it is part of the nephrocystin protein complex. We identified a candidate Plk1 phosphorylation motif (D/E-X-S/T-φ-X-D/E) in nephrocystin-1, and demonstrated in vitro that Plk1 phosphorylates the nephrocystin N-terminus, which includes the specific PLK1 phosphorylation motif. Further, induced disassembly of primary cilia rapidly evoked Plk1 kinase activity, while small molecule inhibition of Plk1 activity or RNAi-mediated downregulation of Plk1 limited the first and second phase of ciliary disassembly. These data identify Plk1 as a novel transition zone signaling protein, suggest a function of Plk1 in cilia dynamics, and link Plk1 to the pathogenesis of NPH and potentially other cystic kidney diseases.
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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.