ArticleMolecular biology of the cell2015
Centrin 3 is an inhibitor of centrosomal Mps1 and antagonizes centrin 2 function.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 21 citations in OpenAlex.
- CETN3 deficiency induces microcephaly by disrupting neural stem/progenitor cell fate through impaired centrosome assembly and RNA splicing.EMBO molecular medicine · 2025Article
- 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
- The Green Valley ofCells · 2022Review
- Structural Basis for the Functional Diversity of Centrins: A Focus on Calcium Sensing Properties and Target Recognition.International journal of molecular sciences · 2021Review
- The sperm centrioles.Molecular and cellular endocrinology · 2020Review
- Article
- Freeing the brake: Proliferation needs primary cilium to disassemble.Journal of biosciences · 2020Review
- A centrosome-localized calcium signal is essential for mammalian cell mitosis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Insights into photoreceptor ciliogenesis revealed by animal models.Progress in retinal and eye research · 2019Review
- Review
- Sfr1, amSphereArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Centrins are a family of small, calcium-binding proteins with diverse cellular functions that play an important role in centrosome biology. We previously identified centrin 2 and centrin 3 (Cetn2 and Cetn3) as substrates of the protein kinase Mps1. However, although Mps1 phosphorylation sites control the function of Cetn2 in centriole assembly and promote centriole overproduction, Cetn2 and Cetn3 are not functionally interchangeable, and we show here that Cetn3 is both a biochemical inhibitor of Mps1 catalytic activity and a biological inhibitor of centrosome duplication. In vitro, Cetn3 inhibits Mps1 autophosphorylation at Thr-676, a known site of T-loop autoactivation, and interferes with Mps1-dependent phosphorylation of Cetn2. The cellular overexpression of Cetn3 attenuates the incorporation of Cetn2 into centrioles and centrosome reduplication, whereas depletion of Cetn3 generates extra centrioles. Finally, overexpression of Cetn3 reduces Mps1 Thr-676 phosphorylation at centrosomes, and mimicking Mps1-dependent phosphorylation of Cetn2 bypasses the inhibitory effect of Cetn3, suggesting that the biological effects of Cetn3 are due to the inhibition of Mps1 function at centrosomes.
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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.