Astrin regulates Aurora-A localization

Biochem Biophys Res Commun. 2008 May 30;370(2):213-9. doi: 10.1016/j.bbrc.2008.03.072. Epub 2008 Mar 24.

Abstract

Alterations in the expression and activity of the centrosomal kinase, Aurora-A/STK15, affect genomic stability, disrupt the fidelity of centrosome duplication, and induce cellular transformation. A mitotic spindle-associated protein, astrin/DEEPEST, was identified as an Aurora-A interacting protein by a two-hybrid screen. Astrin and Aurora-A co-express at mitosis and co-localize to mitotic spindles. RNAi-mediated depletion of astrin abolishes the localization of Aurora-A on mitotic spindles and leads to a moderate mitotic cell cycle delay, which resembles the mitotic arrest phenotypes in siAurora-A treated cells. However, depletion of Aurora-A does not affect astrin localization, and co-depletion of both astrin and Aurora-A causes a mitotic arrest phenotype similar to depletion of siAurora-A alone. These results suggest that astrin acts upstream of Aurora-A to regulate its mitotic spindle localization.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Aurora Kinase A
  • Aurora Kinases
  • Cell Cycle Proteins / analysis
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Centrosome / enzymology
  • Epistasis, Genetic
  • HeLa Cells
  • Humans
  • Mitosis* / drug effects
  • Mitosis* / genetics
  • Protein Serine-Threonine Kinases / analysis
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • RNA Interference
  • Saccharomyces cerevisiae / genetics
  • Spindle Apparatus / enzymology*
  • Two-Hybrid System Techniques

Substances

  • Cell Cycle Proteins
  • SPAG5 protein, human
  • AURKA protein, human
  • Aurora Kinase A
  • Aurora Kinases
  • Protein Serine-Threonine Kinases