Finally, by tracking nucleolar organization and chromatin–chromatin contacts (via 4C analysis), we show that perturbing nuclear organization directly disrupts chromatin organization at mitotic exit. This work highlights the biological significance of spindle pole disassembly at mitotic exit.

NuMA accumulation at spindle poles depends on:
• dynein/dynactin (trucks)
• its coiled-coil domain (cranes), and
• its ability to form multivalent cation-π interactions through its intrinsically disordered region (IDR) at the C-terminus (hooks in cyan).

When Aurora A is inactivated, we found that NuMA, a conserved spindle pole protein, undergoes a material state transition from dynamic to solid, and abnormally accumulates at the spindle poles.
This abnormal “accumulation” causes NuMA segregated chromosomes/nuclei to bend around them.

- We found that Aurora A activity in anaphase is crucial for shaping the nucleus during mitotic exit.
To probe this, we built a cyclin-B1-based degron tool that enables rapid, phase-specific degradation of Aurora A, right as cells exit mitosis.

Happy to share our work in @embojournal 👉 shorturl.at/zXNyn
For decades, we’ve known cells dismantle & rebuild the nuclear envelope in sync with spindle poles. But why does this coordination matter? And how do pole material properties ensure error-free division?
Follow this thread to know more 👇