Phosphorylation of NDRG1 is temporally and spatially controlled during the cell cycle

Biochem Biophys Res Commun. 2011 Jul 29;411(2):227-34. doi: 10.1016/j.bbrc.2011.06.092. Epub 2011 Jun 17.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Cell Cycle*
  • Cell Line, Tumor
  • Centromere / metabolism
  • Down-Regulation
  • Humans
  • Immediate-Early Proteins / metabolism*
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Mitosis
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Cell Cycle Proteins
  • Immediate-Early Proteins
  • Intracellular Signaling Peptides and Proteins
  • N-myc downstream-regulated gene 1 protein
  • Tumor Suppressor Protein p53
  • Protein Serine-Threonine Kinases
  • serum-glucocorticoid regulated kinase