Centrosome-associated NDR kinase regulates centrosome duplication.
Open accessAbstract
Human NDR kinases are upregulated in some cancer types, yet their functions still remain undefined. Here, we report the first known function of a mammalian NDR kinase by demonstrating that human NDR directly contributes to centrosome duplication. A subpopulation of endogenous NDR localizes to centrosomes in a cell-cycle-dependent manner. Overexpression of NDR resulted in centrosome overduplication in a kinase-activity-dependent manner, while expression of kinase-dead NDR or depletion of NDR by small interfering RNA (siRNA) negatively affected centrosome duplication. By targeting NDR to the centrosome, we show that the centrosomal pool of NDR is sufficient to generate supernumerary centrosomes. Furthermore, our data indicate that NDR-driven centrosome duplication requires Cdk2 activity and that Cdk2-induced centrosome amplification is affected upon reduction of NDR activity. Overall, considering that centrosome overduplication is linked to cellular transformation, our observations may also provide a molecular link between mammalian NDR kinases and cancer.
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Mammalian Ndr kinases have been implicated in the regulation of centrosome duplication and in dendrite arborization and spine formation during neuronal development.
“Mammalian Ndr kinases have been implicated in the regulation of centrosome duplication and in dendrite arborization and spine formation during neuronal development (Hergovich et al., 2007; Ultanir et al., 2012).”
From Rassf5 and Ndr kinases act in a novel pathway regulating neuronal polarity through Par3 phosphorylation (2014) · cites this paper as Hergovich et al., 2007
Ndr kinases and Par3 have been implicated in the regulation of centrosome duplication and orientation, respectively.
“Ndr kinases and Par3 have been implicated in the regulation of centrosome duplication and orientation, respectively (Hergovich et al., 2007; Schmoranzer et al., 2009).”
From Rassf5 and Ndr kinases act in a novel pathway regulating neuronal polarity through Par3 phosphorylation (2014) · cites this paper as Hergovich et al., 2007
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- Authors
- Hergovich, A., Lamla, S., Nigg, E. A., & Hemmings, B. A.
- Affiliations
- Friedrich Miescher Institute (CH)
- Max Planck Society (DE)
- Corresponding author
- Hemmings, Brian A.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2007-02
- Volume
- 25
- Issue
- 4
- Pages
- 625-634
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2128413296
- Cited by
- 108
- References
- 33
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 5 · 2023: 1 · 2022: 3 · 2021: 3 · 2020: 5 · 2019: 6 · 2018: 4 · 2017: 6 · 2016: 5 · 2015: 8 · 2014: 7 · 2013: 8 · 2012: 11
- FWCI
- 3.31
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- UCL Discovery (University College London) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- NDR kinase, centrosome duplication, centrosome overduplication, supernumerary centrosomes, CDK2, cell cycle, kinase activity, cancer, cell transformation
- MeSH terms
- Animals, Chlorocebus aethiops, Cricetulus, Cricetinae, HeLa Cells, Humans, Protein Binding, Gene Expression, CHO Cells, Protein Serine-Threonine Kinases, Centrosome, COS Cells, Protein Transport, NIH 3T3 Cells, HCT116 Cells, Cyclin-Dependent Kinase 2, Mice
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