ArticleMolecular biology of the cell2010
Mps1 phosphorylation sites regulate the function of centrin 2 in centriole assembly.
Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 57 citations in OpenAlex.
- MPS1 inhibition as an anticancer strategy: where do we stand?Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026Review
- Spatiotemporal control of cortical centrin patterning by regionalized Sfi1 family scaffolding proteins in Stentor coeruleus.Current biology : CB · 2026Article
- Integrated analysis of hub genes and intrinsically disordered regions in triple-negative breast cancer.Journal, genetic engineering & biotechnology · 2024Article
- CCDC15 localizes to the centriole inner scaffold and controls centriole length and integrity.The Journal of cell biology · 2023Article
- Malaria parasite centrins can assemble by Ca2+-inducible condensation.PLoS pathogens · 2023Article
- Piezo mechanosensory channels regulate centrosome integrity and mitotic entry.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Phosphotyrosine picked threonine kinase stimulates proliferation of human osteosarcoma cellsArchives of medical science : AMS · 2022Article
- Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition.International journal of molecular sciences · 2021Review
- Identification of Metastasis-Associated Biomarkers in Synovial Sarcoma Using Bioinformatics Analysis.Frontiers in genetics · 2020Article
- A robust twelve-gene signature for prognosis prediction of hepatocellular carcinoma.Cancer cell international · 2020Article
- Deletion of both centrin 2 (CETN2) and CETN3 destabilizes the distal connecting cilium of mouse photoreceptors.The Journal of biological chemistry · 2019Article
- TTK promotes mesenchymal signaling via multiple mechanisms in triple negative breast cancer.Oncogenesis · 2018Article
- Review
- Modular elements of the TPR domain in the Mps1 N terminus differentially target Mps1 to the centrosome and kinetochore.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Functional Significance of Aurora Kinases-p53 Protein Family Interactions in Cancer.Frontiers in oncology · 2016Review
- Centrin 3 is an inhibitor of centrosomal Mps1 and antagonizes centrin 2 function.Molecular biology of the cell · 2015Article
- Article
- A putative N-terminal nuclear export sequence is sufficient for Mps1 nuclear exclusion during interphase.BMC cell biology · 2015Article
- Quantitative immunofluorescence assay to measure the variation in protein levels at centrosomes.Journal of visualized experiments : JoVE · 2014Article
- Mad2, Bub3, and Mps1 regulate chromosome segregation and mitotic synchrony in Giardia intestinalis, a binucleate protist lacking an anaphase-promoting complex.Molecular biology of the cell · 2014Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The nondegradable Mps1(Δ12/13) protein drives centriole overproduction, suggesting that Mps1 phosphorylates a subset of centrosomal proteins to drive the assembly of new centrioles. Here we identify three Mps1 phosphorylation sites within the centriolar protein Centrin 2 (Cetn2). Although centrioles can be assembled in the absence of Cetn2, centriole assembly is attenuated in the absence of Cetn2. While wild-type Cetn2 can compensate for this attenuation, a nonphosphorylatable version cannot. In addition, overexpressing Cetn2 causes Mps1-dependent centriole overproduction that requires each of the three Mps1 phosphorylation sites within Cetn2 and is greatly exacerbated by mimicking phosphorylation at any of these sites. Wild-type Cetn2 generates excess foci that are competent as mitotic spindle poles in HsSas-6-depleted cells, suggesting that Cetn2 can organize a subset of centriolar proteins independently of cartwheels. However, centriole overproduction caused by a phosphomimetic Cetn2 mutant requires HsSas-6, suggesting that Cetn2 phosphorylation stimulates the canonical centriole assembly pathway. Moreover, in the absence of Cetn2, Mps1(Δ12/13) cannot drive the production of mature centrioles capable of recruiting γ-Tubulin, and a nonphosphorylatable Cetn2 mutant cannot compensate for this defect and exacerbates Cetn2 depletion. Together, our data suggest that Mps1-dependent phosphorylation of Cetn2 stimulates the canonical centriole assembly pathway.
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