HIPK2 Phosphorylates the Microtubule-Severing Enzyme Spastin at S268 for Abscission

HIPK2 Phosphorylates the Microtubule-Severing Enzyme Spastin at S268 for Abscission

Blog Article

Abscission is the final step of cell division, mediating the LEGO Creator 3-in-1 physical separation of the two daughter cells.A key player in this process is the microtubule-severing enzyme spastin that localizes at the midbody where its activity is crucial to cut microtubules and culminate the cytokinesis.Recently, we demonstrated that HIPK2, a multifunctional kinase involved in several cellular pathways, contributes to abscission and prevents tetraploidization.Here, we show that HIPK2 binds and phosphorylates spastin at serine 268.

During cytokinesis, the midbody-localized spastin is phosphorylated at S268 in HIPK2-proficient cells.In contrast, no spastin is detectable at the midbody in HIPK2-depleted cells.The non-phosphorylatable spastin-S268A mutant does not localize at the midbody and cannot rescue HIPK2-depleted cells from abscission defects.In Optics contrast, the phosphomimetic spastin-S268D mutant localizes at the midbody and restores successful abscission in the HIPK2-depleted cells.

These results show that spastin is a novel target of HIPK2 and that HIPK2-mediated phosphorylation of spastin contributes to its midbody localization for successful abscission.