ASB7 regulates spindle dynamics and genome integrity by targeting DDA3 for proteasomal degradation

J Cell Biol. 2016 Oct 10;215(1):95-106. doi: 10.1083/jcb.201603062. Epub 2016 Oct 3.


Proper dynamic regulation of the spindle is essential for successful cell division. However, the molecular mechanisms that regulate spindle dynamics in mitosis are not fully understood. In this study, we show that Cullin 5-interacting suppressor of cytokine signaling box protein ASB7 ubiquitinates DDA3, a regulator of spindle dynamics, thereby targeting it for proteasomal degradation. The presence of microtubules (MTs) prevented the ASB7-DDA3 interaction, thus stabilizing DDA3. Knockdown of ASB7 decreased MT polymerization and increased the proportion of cells with unaligned chromosomes, and this phenotype was rescued by deletion of DDA3. Collectively, these data indicate that ASB7 plays a crucial role in regulating spindle dynamics and genome integrity by controlling the expression of DDA3.

MeSH terms

  • Ankyrins / metabolism*
  • Cell Cycle
  • Cell Division
  • Cullin Proteins / metabolism
  • Genome, Human
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Microtubules / metabolism
  • Models, Biological
  • Phosphoproteins / metabolism*
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Binding
  • Protein Stability
  • Proteolysis*
  • Spindle Apparatus / metabolism*
  • Ubiquitination


  • ASB7 protein, human
  • Ankyrins
  • CUL5 protein, human
  • Cullin Proteins
  • PSRC1 protein, human
  • Phosphoproteins
  • Proteasome Endopeptidase Complex

Associated data

  • RefSeq/NM_032636
  • RefSeq/NM_198243
  • RefSeq/NM_001098511