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High expression level of NEK9 is associated with recurrence in glioblastoma.
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Signaling cascade of the NIMA-related kinases (Neks) Nek6, Nek7, and Nek9 is required for the localization and function of two kinesins essential for cytokinesis, Mklp2 and Kif14 to properly coordinate cytokinesis.
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Recessive NEK9 mutation is associated with lethal skeletal dysplasia.
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Somatic Mutations in NEK9 Cause Nevus Comedonicus.
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Overall, these results highlight the complexity of virus-host interactions and identify a new role for the cellular protein Nek9 during human adenovirus infection, suggesting a role for Nek9 in regulating p53 target gene expression.
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The C-terminal domain of Nek9 activates Nek7 through promoting back-to-back dimerization.
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The findings demonstrate that a novel NEK9 network regulates the growth of cancer cells lacking functional p53.
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NEK9 inhibition represents a novel anti-cancer strategy by induction of mitotic catastrophe via impairment of spindle dynamics, cytokinesis and mitotic checkpoint control.
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Structural analysis of LC8 with both Nek9 peptides, together with different biophysical experiments, explains the observed diminished binding affinity of Nek9 to LC8 upon phosphorylation on Ser(944) within the Nek9 sequence
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Nek9 phosphorylates NEDD1 on Ser377 driving its recruitment and thereby that of gamma-tubulin to the centrosome in mitotic cells.
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The interaction between the human NimA-like protein kinase Nek9 and the Helicobacter HcpC has been validated by ELISA and surface plasmon resonance.
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Nek9 is a Plk1-activated kinase that controls early centrosome separation through Nek6/7 and Eg5.
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DYNLL/LC8 protein controls signal transduction through the Nek9/Nek6 signaling module by regulating Nek6 binding to Nek9.
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binds the Ran GTPase and regulates mitotic progression
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Activated in mitosis, and activates nek6 and nek7 kinase.
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mediates certain cellular processes, which are ultimately essential for interphase progression
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The disruption of a nuclear function of NEK9 by adenovirus E1A-associated cellular proteins is reported.
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The activity of Nek6 and Nek7, but not the tyrosine mutant, is increased by interaction with the Nek9 noncatalytic C-terminal domain, suggesting a mechanism in which the tyrosine is released from its autoinhibitory position.
