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Updated: May 31, 2026

Studying Cell Cycle-regulated Gene Expression by Two Complementary Cell Synchronization Protocols
Published on: June 6, 2017
Phosphorylation of NDRG1 is temporally and spatially controlled during the cell cycle
Catherine McCaig1, Louisa Potter, Olga Abramczyk
1Centre for Cancer Research & Cell Biology, School of Medicine, Dentistry & Biomedical Sciences, Queen's University Belfast, CCRCB Building, 97 Lisburn Road, Belfast, BT9 7BL, UK.
Abstract:
The tumour metastasis suppressor, N-myc Downstream Regulated Gene (NDRG) 1, is a by the protein kinases SGK1 and GSK3β, but the relevance of its phosphorylation remains unclear. Analysis of HCT116 cells, either proficient or deficient for p53 revealed NDRG1 protein expression and phosphorylation by SGK1 was increased basally in p53-deficient cells. Treatment with the cell cycle inhibitors, aphidicolin or nocodazole also revealed increased NDRG1 phosphorylation in p53-deficient cells. Finally, phosphorylated NDRG1 was found to co-localise with γ-tubulin on centromeres and also to the cleavage furrow during cytokinesis. Taken together, this work demonstrates that NDRG1 phosphorylation, by the protein kinase SGK1, is temporally and spatially controlled during the cell cycle, suggesting a role for NDRG1 in successful mitosis.
Insights
The N-myc Downstream Regulated Gene (NDRG) 1 protein
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- The tumor metastasis suppressor NDRG1 (N-myc Downstream Regulated Gene 1) is phosphorylated by SGK1 and GSK3β.
- The functional significance of NDRG1 phosphorylation in cellular processes remains largely unknown.
Purpose of the Study:
- To investigate the regulation and cell cycle-specific localization of NDRG1 phosphorylation.
- To explore the role of p53 status in modulating NDRG1 phosphorylation by SGK1.
Main Methods:
- Western blotting to detect NDRG1 and its phosphorylation.
- Analysis of HCT116 cells with varying p53 proficiency.
- Treatment with cell cycle inhibitors (aphidicolin, nocodazole).
- Immunofluorescence microscopy to determine subcellular localization.
Main Results:
- NDRG1 protein expression and SGK1-mediated phosphorylation were elevated in p53-deficient cells.
- Cell cycle inhibition further increased NDRG1 phosphorylation in p53-deficient cells.
- Phosphorylated NDRG1 localized to centromeres and the cleavage furrow during cytokinesis.
Conclusions:
- SGK1-mediated NDRG1 phosphorylation is regulated by p53 status and cell cycle progression.
- Phosphorylated NDRG1 exhibits specific temporal and spatial localization during mitosis.
- These findings suggest a role for NDRG1 phosphorylation in ensuring successful cell division and mitosis.
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